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Conserved domains on  [gi|300538089|emb|CBU87017|]
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unnamed protein product [Homo sapiens]

Protein Classification

pyruvate carboxylase( domain architecture ID 11437128)

pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second; catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
35-1177 0e+00

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


:

Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 1955.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   35 KPIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAV 114
Cdd:COG1038     2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  115 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFK 194
Cdd:COG1038    82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  195 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 274
Cdd:COG1038   162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  275 VEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEG 354
Cdd:COG1038   242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  355 RSL--PDLGL-RQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIA 431
Cdd:COG1038   322 YSLddPEIGIpSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVTA 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  432 HGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNG 511
Cdd:COG1038   402 WGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVNG 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  512 PTTpIPVKASPSPTDPVVPAVPI-GPPPAGFRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKI 590
Cdd:COG1038   482 PPG-VKGRPKPDFPKPKLPKVDLgAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  591 APYVAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENG 670
Cdd:COG1038   561 APATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEAG 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  671 MDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDMAGLLKPT 750
Cdd:COG1038   641 IDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKPY 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  751 ACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMER 830
Cdd:COG1038   721 AAYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLDA 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  831 VFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPS 910
Cdd:COG1038   800 LQELSNYWEAVRKYYAPFE--SGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPS 877
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  911 SKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQAL 990
Cdd:COG1038   878 SKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDAL 957
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  991 EKELVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNR 1070
Cdd:COG1038   958 RAELEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDE 1037
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089 1071 AGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVT 1150
Cdd:COG1038  1038 DGMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTIT 1117
                        1130      1140
                  ....*....|....*....|....*..
gi 300538089 1151 SPMEGTVRKVHVTKDMTLEGDDLILEI 1177
Cdd:COG1038  1118 APRDGTVKEVLVKEGDQVEAGDLLIEL 1144
 
Name Accession Description Interval E-value
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
35-1177 0e+00

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 1955.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   35 KPIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAV 114
Cdd:COG1038     2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  115 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFK 194
Cdd:COG1038    82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  195 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 274
Cdd:COG1038   162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  275 VEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEG 354
Cdd:COG1038   242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  355 RSL--PDLGL-RQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIA 431
Cdd:COG1038   322 YSLddPEIGIpSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVTA 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  432 HGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNG 511
Cdd:COG1038   402 WGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVNG 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  512 PTTpIPVKASPSPTDPVVPAVPI-GPPPAGFRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKI 590
Cdd:COG1038   482 PPG-VKGRPKPDFPKPKLPKVDLgAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  591 APYVAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENG 670
Cdd:COG1038   561 APATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEAG 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  671 MDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDMAGLLKPT 750
Cdd:COG1038   641 IDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKPY 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  751 ACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMER 830
Cdd:COG1038   721 AAYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLDA 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  831 VFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPS 910
Cdd:COG1038   800 LQELSNYWEAVRKYYAPFE--SGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPS 877
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  911 SKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQAL 990
Cdd:COG1038   878 SKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDAL 957
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  991 EKELVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNR 1070
Cdd:COG1038   958 RAELEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDE 1037
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089 1071 AGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVT 1150
Cdd:COG1038  1038 DGMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTIT 1117
                        1130      1140
                  ....*....|....*....|....*..
gi 300538089 1151 SPMEGTVRKVHVTKDMTLEGDDLILEI 1177
Cdd:COG1038  1118 APRDGTVKEVLVKEGDQVEAGDLLIEL 1144
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
33-1178 0e+00

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 1850.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   33 EYKPIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVD 112
Cdd:PRK12999    1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  113 AVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPII 192
Cdd:PRK12999   81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  193 FKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQ 272
Cdd:PRK12999  161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  273 KVVEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVA 352
Cdd:PRK12999  241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  353 EGRSLPDLG---LRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKV 429
Cdd:PRK12999  321 EGATLHDLEigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  430 IAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMV 509
Cdd:PRK12999  401 TAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTV 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  510 NGPttPIPVKASPSPTDPVVPAVPIG-PPPAGFRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLK 588
Cdd:PRK12999  481 NGF--PGVKKKPPVFPDPRLPKVDLSaPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLL 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  589 KIAPYVAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKE 668
Cdd:PRK12999  559 RIAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAA 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  669 NGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDMAGLLK 748
Cdd:PRK12999  639 AGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLK 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  749 PTACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPM 828
Cdd:PRK12999  719 PAAAYELVSALKEEV-DLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDL 797
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  829 ERVFDYSEYWEGARGLYAAFdcTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVT 908
Cdd:PRK12999  798 DAIRKLSPYWEAVRPYYAPF--ESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVT 875
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  909 PSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQ 988
Cdd:PRK12999  876 PSSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFE 955
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  989 ALEKELVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDL 1068
Cdd:PRK12999  956 AERAELEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEP 1035
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089 1069 NRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETV 1148
Cdd:PRK12999 1036 DEDGMRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETT 1115
                        1130      1140      1150
                  ....*....|....*....|....*....|
gi 300538089 1149 VTSPMEGTVRKVHVTKDMTLEGDDLILEIE 1178
Cdd:PRK12999 1116 ITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
39-1178 0e+00

pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 130302 [Multi-domain]  Cd Length: 1143  Bit Score: 1743.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089    39 KVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRG--LAPVQAYLHIPDIIKVAKENNVDAVHP 116
Cdd:TIGR01235    1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAA 196
Cdd:TIGR01235   81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:TIGR01235  161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   277 IAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRS 356
Cdd:TIGR01235  241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   357 LP--DLGL-RQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIAHG 433
Cdd:TIGR01235  321 LPtpQLGVpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   434 KDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGpT 513
Cdd:TIGR01235  401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNG-H 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   514 TPIPVKASPSPTDPVVPAVPI--GPPPAGFRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIA 591
Cdd:TIGR01235  480 PEAKDKLKPLENAPRVVVLYAdqNPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIA 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   592 PYVAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGM 671
Cdd:TIGR01235  560 PTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGI 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   672 DVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDMAGLLKPTA 751
Cdd:TIGR01235  640 DIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAA 719
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   752 CTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERV 831
Cdd:TIGR01235  720 AKLLIKALREKT-DLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWI 798
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   832 FDYSEYWEGARGLYAAFDCtaTMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSS 911
Cdd:TIGR01235  799 RELSAYWEAVRNLYAAFES--DLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSS 876
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   912 KIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQALE 991
Cdd:TIGR01235  877 KVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIR 956
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   992 KELVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRA 1071
Cdd:TIGR01235  957 KDLQEKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQ 1036
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  1072 GQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTS 1151
Cdd:TIGR01235 1037 GEREVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQA 1116
                         1130      1140
                   ....*....|....*....|....*..
gi 300538089  1152 PMEGTVRKVHVTKDMTLEGDDLILEIE 1178
Cdd:TIGR01235 1117 PKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
DRE_TIM_PC_TC_5S cd07937
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ...
565-848 8.05e-161

Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163675  Cd Length: 275  Bit Score: 478.46  E-value: 8.05e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  565 LMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFskLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 644
Cdd:cd07937     1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  645 GANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDvadpsrTKYSLQYYM 724
Cdd:cd07937    79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  725 GLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPdLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGM 804
Cdd:cd07937   153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 300538089  805 TSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAF 848
Cdd:cd07937   232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
PYC_OADA pfam02436
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ...
861-1061 8.33e-95

Conserved carboxylase domain; This domain represents a conserved region in pyruvate carboxylase (PYC), oxaloacetate decarboxylase alpha chain (OADA), and transcarboxylase 5s subunit. The domain is found adjacent to the HMGL-like domain (pfam00682) and often close to the biotin_lipoyl domain (pfam00364) of biotin requiring enzymes.


Pssm-ID: 460557 [Multi-domain]  Cd Length: 201  Bit Score: 300.91  E-value: 8.33e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   861 VYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSF 940
Cdd:pfam02436    1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   941 PRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHF 1020
Cdd:pfam02436   81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 300538089  1021 KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIK 1061
Cdd:pfam02436  161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
375-482 2.86e-49

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 214878 [Multi-domain]  Cd Length: 107  Bit Score: 169.90  E-value: 2.86e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089    375 QCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRG 454
Cdd:smart00878    1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVD-SGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
                            90       100
                    ....*....|....*....|....*...
gi 300538089    455 VKTNIAFLQNVLNNQQFLAGTVDTQFID 482
Cdd:smart00878   80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
 
Name Accession Description Interval E-value
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
35-1177 0e+00

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 1955.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   35 KPIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAV 114
Cdd:COG1038     2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  115 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFK 194
Cdd:COG1038    82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  195 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 274
Cdd:COG1038   162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  275 VEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEG 354
Cdd:COG1038   242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  355 RSL--PDLGL-RQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIA 431
Cdd:COG1038   322 YSLddPEIGIpSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVTA 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  432 HGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNG 511
Cdd:COG1038   402 WGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVNG 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  512 PTTpIPVKASPSPTDPVVPAVPI-GPPPAGFRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKI 590
Cdd:COG1038   482 PPG-VKGRPKPDFPKPKLPKVDLgAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  591 APYVAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENG 670
Cdd:COG1038   561 APATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEAG 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  671 MDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDMAGLLKPT 750
Cdd:COG1038   641 IDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKPY 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  751 ACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMER 830
Cdd:COG1038   721 AAYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLDA 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  831 VFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPS 910
Cdd:COG1038   800 LQELSNYWEAVRKYYAPFE--SGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPS 877
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  911 SKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQAL 990
Cdd:COG1038   878 SKVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDAL 957
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  991 EKELVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNR 1070
Cdd:COG1038   958 RAELEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDE 1037
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089 1071 AGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVT 1150
Cdd:COG1038  1038 DGMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTIT 1117
                        1130      1140
                  ....*....|....*....|....*..
gi 300538089 1151 SPMEGTVRKVHVTKDMTLEGDDLILEI 1177
Cdd:COG1038  1118 APRDGTVKEVLVKEGDQVEAGDLLIEL 1144
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
33-1178 0e+00

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 1850.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   33 EYKPIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVD 112
Cdd:PRK12999    1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  113 AVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPII 192
Cdd:PRK12999   81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  193 FKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQ 272
Cdd:PRK12999  161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  273 KVVEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVA 352
Cdd:PRK12999  241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  353 EGRSLPDLG---LRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKV 429
Cdd:PRK12999  321 EGATLHDLEigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  430 IAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMV 509
Cdd:PRK12999  401 TAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTV 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  510 NGPttPIPVKASPSPTDPVVPAVPIG-PPPAGFRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLK 588
Cdd:PRK12999  481 NGF--PGVKKKPPVFPDPRLPKVDLSaPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLL 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  589 KIAPYVAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKE 668
Cdd:PRK12999  559 RIAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAA 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  669 NGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDMAGLLK 748
Cdd:PRK12999  639 AGIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLK 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  749 PTACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPM 828
Cdd:PRK12999  719 PAAAYELVSALKEEV-DLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDL 797
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  829 ERVFDYSEYWEGARGLYAAFdcTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVT 908
Cdd:PRK12999  798 DAIRKLSPYWEAVRPYYAPF--ESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVT 875
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  909 PSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQ 988
Cdd:PRK12999  876 PSSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFE 955
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  989 ALEKELVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDL 1068
Cdd:PRK12999  956 AERAELEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEP 1035
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089 1069 NRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETV 1148
Cdd:PRK12999 1036 DEDGMRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETT 1115
                        1130      1140      1150
                  ....*....|....*....|....*....|
gi 300538089 1149 VTSPMEGTVRKVHVTKDMTLEGDDLILEIE 1178
Cdd:PRK12999 1116 ITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
39-1178 0e+00

pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 130302 [Multi-domain]  Cd Length: 1143  Bit Score: 1743.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089    39 KVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRG--LAPVQAYLHIPDIIKVAKENNVDAVHP 116
Cdd:TIGR01235    1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAA 196
Cdd:TIGR01235   81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:TIGR01235  161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   277 IAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRS 356
Cdd:TIGR01235  241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   357 LP--DLGL-RQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIAHG 433
Cdd:TIGR01235  321 LPtpQLGVpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   434 KDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGpT 513
Cdd:TIGR01235  401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNG-H 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   514 TPIPVKASPSPTDPVVPAVPI--GPPPAGFRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIA 591
Cdd:TIGR01235  480 PEAKDKLKPLENAPRVVVLYAdqNPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIA 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   592 PYVAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGM 671
Cdd:TIGR01235  560 PTTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGI 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   672 DVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLQYYMGLAEELVRAGTHILCIKDMAGLLKPTA 751
Cdd:TIGR01235  640 DIFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAA 719
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   752 CTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERV 831
Cdd:TIGR01235  720 AKLLIKALREKT-DLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWI 798
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   832 FDYSEYWEGARGLYAAFDCtaTMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSS 911
Cdd:TIGR01235  799 RELSAYWEAVRNLYAAFES--DLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSS 876
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   912 KIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQALE 991
Cdd:TIGR01235  877 KVVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIR 956
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   992 KELVDRHGEEVTPEDVLSAAMYPDVFAHFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRA 1071
Cdd:TIGR01235  957 KDLQEKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQ 1036
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  1072 GQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTS 1151
Cdd:TIGR01235 1037 GEREVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQA 1116
                         1130      1140
                   ....*....|....*....|....*..
gi 300538089  1152 PMEGTVRKVHVTKDMTLEGDDLILEIE 1178
Cdd:TIGR01235 1117 PKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
36-497 0e+00

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 711.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   36 PIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENNVDAVH 115
Cdd:COG4770     1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIG-PAPAAESYLNIDAIIAAAKATGADAIH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  116 PGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKA 195
Cdd:COG4770    80 PGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  196 AYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVV 275
Cdd:COG4770   160 SAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  276 EIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGR 355
Cdd:COG4770   240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  356 SLPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKD 435
Cdd:COG4770   320 PLP---FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSMIAKLIVWGPD 395
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300538089  436 HPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRA 497
Cdd:COG4770   396 REEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
37-484 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 627.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   37 IKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPvQAYLHIPDIIKVAKENNVDAVHP 116
Cdd:PRK08591    2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSK-KSYLNIPAIISAAEITGADAIHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAA 196
Cdd:PRK08591   81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:PRK08591  161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  277 IAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRS 356
Cdd:PRK08591  241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  357 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 436
Cdd:PRK08591  321 LS---IKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHGETR 396
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 300538089  437 PTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDEN 484
Cdd:PRK08591  397 EEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
38-487 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 582.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   38 KKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENNVDAVHPG 117
Cdd:PRK08654    3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPA-PPSKSYLNIERIIDVAKKAGADAIHPG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  118 YGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAAY 197
Cdd:PRK08654   82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  198 GGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEI 277
Cdd:PRK08654  162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  278 APAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDrHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSL 357
Cdd:PRK08654  242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  358 PdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHP 437
Cdd:PRK08654  321 S---FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVD-SGVHMGYEIPPYYDSMISKLIVWGRTRE 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 300538089  438 TAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPEL 487
Cdd:PRK08654  397 EAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
37-481 0e+00

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 564.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   37 IKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENNVDAVHP 116
Cdd:PRK06111    2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIG-GPRVQESYLNLEKIIEIAKKTGAEAIHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAA 196
Cdd:PRK06111   81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:PRK06111  161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  277 IAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRS 356
Cdd:PRK06111  241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  357 LPdlgLRQENIRINGCAIQCRVTTEDPaRSFQPDTGRIEVFRSGEGMGIRLDNASAfQGAVISPHYDSLLVKVIAHGKDH 436
Cdd:PRK06111  321 LS---FTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMIAKLIAHGETR 395
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 300538089  437 PTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFI 481
Cdd:PRK06111  396 EEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
37-489 5.59e-178

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 531.21  E-value: 5.59e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   37 IKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGlaPVQAYLHIPDIIKVAKENNVDAVHP 116
Cdd:PRK07178    2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD--PLAGYLNPRRLVNLAVETGCDALHP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAA 196
Cdd:PRK07178   80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:PRK07178  160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  277 IAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRS 356
Cdd:PRK07178  240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  357 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 436
Cdd:PRK07178  320 LS---YKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTA-IYTGYTIPPYYDSMCAKLIVWALTW 395
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 300538089  437 PTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFQ 489
Cdd:PRK07178  396 EEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTN 448
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
37-484 2.02e-177

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 528.90  E-value: 2.02e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   37 IKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENNVDAVHP 116
Cdd:PRK05586    2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPA-SSKDSYLNIQNIISATVLTGAQAIHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAA 196
Cdd:PRK05586   81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:PRK05586  161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  277 IAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRS 356
Cdd:PRK05586  241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  357 lpdLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 436
Cdd:PRK05586  321 ---LSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSA-VYSGYTIPPYYDSMIGKLIVYGKDR 396
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 300538089  437 PTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDEN 484
Cdd:PRK05586  397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKK 444
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
37-483 1.85e-174

acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129605 [Multi-domain]  Cd Length: 449  Bit Score: 521.24  E-value: 1.85e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089    37 IKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENNVDAVHP 116
Cdd:TIGR00514    2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPA-PSAKSYLNIPNIISAAEITGADAIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAA 196
Cdd:TIGR00514   81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   197 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 276
Cdd:TIGR00514  161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   277 IAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRS 356
Cdd:TIGR00514  241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   357 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 436
Cdd:TIGR00514  321 LS---LKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSH-VYSGYTVPPYYDSMIGKLITYGKTR 396
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 300538089   437 PTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDE 483
Cdd:TIGR00514  397 EVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
35-482 2.36e-162

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 490.42  E-value: 2.36e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   35 KPIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPvQAYLHIPDIIKVAKENNVDAV 114
Cdd:PRK12833    3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAA-KSYLNPAAILAAARQCGADAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  115 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFK 194
Cdd:PRK12833   82 HPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  195 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYgNILHLYERDCSIQRRHQKV 274
Cdd:PRK12833  162 AAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  275 VEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRH-GKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAE 353
Cdd:PRK12833  241 LEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDArGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIAD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  354 GRSlpdLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHG 433
Cdd:PRK12833  321 GEP---LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVD-SLLYPGYRVPPFYDSLLAKLIVHG 396
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 300538089  434 KDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFID 482
Cdd:PRK12833  397 EDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
DRE_TIM_PC_TC_5S cd07937
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ...
565-848 8.05e-161

Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163675  Cd Length: 275  Bit Score: 478.46  E-value: 8.05e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  565 LMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFskLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 644
Cdd:cd07937     1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  645 GANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDvadpsrTKYSLQYYM 724
Cdd:cd07937    79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  725 GLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPdLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGM 804
Cdd:cd07937   153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 300538089  805 TSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAF 848
Cdd:cd07937   232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
35-484 1.56e-157

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 476.93  E-value: 1.56e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   35 KPIKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENNVDAV 114
Cdd:PRK08462    2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIG-GAKSSESYLNIPAIISAAEIFEADAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  115 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFK 194
Cdd:PRK08462   81 FPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  195 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 274
Cdd:PRK08462  161 AAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  275 VEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEG 354
Cdd:PRK08462  241 IEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  355 RSLPDlglrQENIRINGCAIQCRVTTEDPaRSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGK 434
Cdd:PRK08462  321 EELPS----QESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMD-SHAYAGYVVPPYYDSMIGKLIVWGE 394
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 300538089  435 DHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDEN 484
Cdd:PRK08462  395 DRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
37-499 1.12e-155

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 473.53  E-value: 1.12e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   37 IKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGlaPVQAYLHIPDIIKVAKENNVDAVHP 116
Cdd:PRK08463    2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTD--PIKGYLDVKRIVEIAKACGADAIHP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  117 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDaPIT--SLHEAHEFSNTYGFPIIFK 194
Cdd:PRK08463   80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTE-KLNseSMEEIKIFARKIGYPVILK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  195 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 274
Cdd:PRK08463  159 ASGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  275 VEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEG 354
Cdd:PRK08463  239 IEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  355 RSLPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGK 434
Cdd:PRK08463  319 EILD---LEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVD-SHIYKDYTIPPYYDSMLAKLIVKAT 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300538089  435 DHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQFIDENPELFqLRPAQNRAQK 499
Cdd:PRK08463  395 SYDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQEL-LEKTEDRHQE 458
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
567-1178 1.74e-153

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 472.02  E-value: 1.74e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  567 DTTFRDAHQSLLATRVRTHDLKKIApyvahnfSKL-----FSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQM 641
Cdd:PRK09282    8 DTTLRDAHQSLLATRMRTEDMLPIA-------EKLdkvgfWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  642 LLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLQ 721
Cdd:PRK09282   81 LLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT---TSPVHT---IE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  722 YYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSM 801
Cdd:PRK09282  155 KYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEV-DLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISPL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  802 SGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAFDCTATMksGNSDVYENEIPGGQYTNLHFQAHSM 881
Cdd:PRK09282  234 AFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTI--VDTRVLIHQVPGGMISNLVSQLKEQ 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  882 GLGSKFKEVKK--AYVEANqmLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGYIGVPHGGF 959
Cdd:PRK09282  312 NALDKLDEVLEeiPRVRED--LGYPPLVTPTSQIVGTQAVLNVLTG-ERYK--------VITKEVKDYVKGLYGRPPAPI 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  960 PEPFRSKVLKDLPRVEGRPGASLPPlDLQALEKELVDRHGEEvtPEDVLSAAMYPDV----FAHFKDFTATFGPLDSLNT 1035
Cdd:PRK09282  381 NEELRKKIIGDEEPITCRPADLLEP-ELEKARKEAEELGKSE--KEDVLTYALFPQIakkfLEEREAGELKPEPEPKEAA 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089 1036 RlfLQGPKIAEEFEVELErGKTLHIKALAVSdlnRAGQRQVFFELNGQLRSILVkdtQAMKEMHFHPKALKDVKGQIGAP 1115
Cdd:PRK09282  458 A--AGAEGIPTEFKVEVD-GEKYEVKIEGVK---AEGKRPFYLRVDGMPEEVVV---EPLKEIVVGGRPRASAPGAVTSP 528
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300538089 1116 MPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE 1178
Cdd:PRK09282  529 MPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
OadA1 COG5016
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ...
563-1016 3.03e-127

Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate/oxaloacetate carboxyltransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 444040 [Multi-domain]  Cd Length: 540  Bit Score: 400.81  E-value: 3.03e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  563 LLLMDTTFRDAHQSLLATRVRTHDLKKIAPY-VAHNFsklFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQM 641
Cdd:COG5016     4 VKITDTTLRDGHQSLFATRMRTEDMLPIAEKlDEAGF---WSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  642 LLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVAdpsrtkYSLQ 721
Cdd:COG5016    81 LLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYTISPV------HTVE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  722 YYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSM 801
Cdd:COG5016   155 YYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEAL-DIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  802 SGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAFDCTATMKsgNSDVYENEIPGGQYTNLHFQAHSM 881
Cdd:COG5016   234 AGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGV--DPRVLVHQVPGGMLSNLVSQLKEQ 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  882 GLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGYIGVPHGGFPE 961
Cdd:COG5016   312 GALDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG-ERYK--------MITKEVKDYVLGYYGKTPAPIDP 382
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 300538089  962 PFRSKVLKDLPRVEGRPGASLPPlDLQALEKElvdrhGEEVTPEDVLSAAMYPDV 1016
Cdd:COG5016   383 EVRKKALGDEEPITCRPADLLEP-ELEKLRKE-----GLAKSDEDVLTYALFPQV 431
oadA TIGR01108
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ...
567-1168 1.82e-125

oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate decarboxylase alpha subunit and its equivalents in archaea. The oxaloacetate decarboxylase Na+ pump is the paradigm of the family of Na+ transport decarboxylases that present in bacteria and archaea. It a multi subunit enzyme consisting of a peripheral alpha-subunit and integral membrane subunits beta and gamma. The energy released by the decarboxylation reaction of oxaloacetate is coupled to Na+ ion pumping across the membrane. [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Other]


Pssm-ID: 273447 [Multi-domain]  Cd Length: 582  Bit Score: 397.62  E-value: 1.82e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   567 DTTFRDAHQSLLATRVRTHDLKKIAPyvAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGA 646
Cdd:TIGR01108    3 DVVLRDAHQSLFATRMRTEDMLPIAE--KLDDVGYWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQMLLRGQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   647 NAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLQYYMGL 726
Cdd:TIGR01108   81 NLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT---TSPVHT---LETYLDL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   727 AEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGMTS 806
Cdd:TIGR01108  155 AEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRF-GLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSMSGGTS 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   807 QPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSK 886
Cdd:TIGR01108  234 HPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFE--GQLKGPDSRILVAQVPGGMLSNLESQLKEQNALDK 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   887 FKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEAEAqaeelsfpRSVVEFLQGYIGVPHGGFPEPFRSK 966
Cdd:TIGR01108  312 LDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG-ERYKTIT--------KETKGYLKGEYGRTPAPINAELQRK 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   967 VLKDL-PRVEGRPGASLPPlDLQALEKELVDRHGEEVTPEDVLSAAMYPDVfahfkdftatfgpldslnTRLFLQGPKIA 1045
Cdd:TIGR01108  383 ILGDEkPIVDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQV------------------GLKFLENRHNP 443
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  1046 EEFE--VELERGKTLHIKAlAVSDLNRAGQRQVFFELNGQLRSILVKD-------TQAMKEMHFHPKALKDVK--GQIGA 1114
Cdd:TIGR01108  444 AAFEpkPEEKVIEQEHAQV-VGKYEETHASGSYTVEVEGKAFVVKVSPggdvsqiTASAPANTSGGTVAAKAGagTPVTA 522
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  1115 PMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKV------HVTKDMTL 1168
Cdd:TIGR01108  523 PIAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREIlvkvgdAVSVGQVL 582
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
563-1171 2.42e-101

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 333.44  E-value: 2.42e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  563 LLLMDTTFRDAHQSLLATRVRTHDLKKIAPyvahnfsKL-----FSMENWGGATFDVAMRFLYECPWRRLQELRELIPNI 637
Cdd:PRK14040    5 LAITDVVLRDAHQSLFATRLRLDDMLPIAA-------KLdkvgyWSLESWGGATFDACIRFLGEDPWERLRELKKAMPNT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  638 PFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTk 717
Cdd:PRK14040   78 PQQMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT---TSPVHT- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  718 ysLQYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVA 797
Cdd:PRK14040  154 --LQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRV-DVPLHLHCHATTGLSTATLLKAIEAGIDGVDTA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  798 ADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQ 877
Cdd:PRK14040  231 ISSMSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFE--GQLKGVDSRILVAQVPGGMLTNMESQ 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  878 AHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGyigvPHG 957
Cdd:PRK14040  309 LKEQGAADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQAVLNVLTG-ERYK--------TITKETAGVLKG----EYG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  958 GFPEPF----RSKVLKDLPRVEGRPGASLPPlDLQALEKELVDRHGE------EVTPEDVLSAAMYPDV---FAHFKDFT 1024
Cdd:PRK14040  376 ATPAPVnaelQARVLEGAEPITCRPADLLAP-ELDKLEAELRRQAQEkgitlaENAIDDVLTYALFPQIglkFLENRHNP 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089 1025 ATFGPLDSL-NTRLFLQGPKIAEE-FEVELErGKTLHIKalaVSDlnragqrqvffelNGQLRSILVKDTQAMKEMHFHP 1102
Cdd:PRK14040  455 AAFEPVPQAeAAQPAAKAEPAGSEtYTVEVE-GKAYVVK---VSE-------------GGDISQITPAAPAAAPAAAAAA 517
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300538089 1103 KALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTkdmtlEGD 1171
Cdd:PRK14040  518 APAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVK-----EGD 581
PRK12331 PRK12331
oxaloacetate decarboxylase subunit alpha;
565-1023 5.73e-96

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 183446 [Multi-domain]  Cd Length: 448  Bit Score: 313.95  E-value: 5.73e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  565 LMDTTFRDAHQSLLATRVRTHDLKKIApyvahnfSKL-----FSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPF 639
Cdd:PRK12331    6 ITETVLRDGQQSLIATRMTTEEMLPIL-------EKLdnagyHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  640 QMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkys 719
Cdd:PRK12331   79 QMLLRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT---TSPVHT--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  720 LQYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFpDLPLHIHTHDTSgaGVAAM--LACAQAGADVVDVA 797
Cdd:PRK12331  153 IDYFVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAV-TVPLEVHTHATS--GIAEMtyLKAIEAGADIIDTA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  798 ADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLY-AAFDCTATMKSGNSDVYENEIPGGQYTNLHF 876
Cdd:PRK12331  230 ISPFAGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYrEEGILNPKVKDVEPKTLIYQVPGGMLSNLLS 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  877 QAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEAeaqaeelsFPRSVVEFLQGYIGVPH 956
Cdd:PRK12331  310 QLKEQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALMNVISG-ERYKM--------VPNEIKDYVRGLYGRPP 380
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300538089  957 GGFPEPFRSKVLKDLPRVEGRPGASLPPlDLQALEKELVDRHGEEvtpEDVLSAAMYPDVfahFKDF 1023
Cdd:PRK12331  381 APIAEEIKKKIIGDEEVITCRPADLIEP-QLEKLREEIAEYAESE---EDVLSYALFPQQ---AKDF 440
PYC_OADA pfam02436
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ...
861-1061 8.33e-95

Conserved carboxylase domain; This domain represents a conserved region in pyruvate carboxylase (PYC), oxaloacetate decarboxylase alpha chain (OADA), and transcarboxylase 5s subunit. The domain is found adjacent to the HMGL-like domain (pfam00682) and often close to the biotin_lipoyl domain (pfam00364) of biotin requiring enzymes.


Pssm-ID: 460557 [Multi-domain]  Cd Length: 201  Bit Score: 300.91  E-value: 8.33e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   861 VYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSF 940
Cdd:pfam02436    1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   941 PRSVVEFLQGYIGVPHGGFPEPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHF 1020
Cdd:pfam02436   81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 300538089  1021 KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIK 1061
Cdd:pfam02436  161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
564-1178 5.51e-91

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 305.11  E-value: 5.51e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  564 LLMDTTFRDAHQSLLATRVRTHDLKKIAPYVahNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLL 643
Cdd:PRK14042    5 FITDVTLRDAHQCLIATRMRTEDMLPICNKM--DDVGFWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQLSMLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  644 RGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvadpSRTKYSLQYY 723
Cdd:PRK14042   83 RGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT------TSPVHTLDNF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  724 MGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRdRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSG 803
Cdd:PRK14042  157 LELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLK-QATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  804 MTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAFDCTATMKSGNSDVYenEIPGGQYTNLHFQAHSMGL 883
Cdd:PRK14042  236 GASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLY--QVPGGMISNLYNQLKEQNA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  884 GSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlsraeaeaqAEELSFPRSVVEFLQGYIGVPHGGFPEPF 963
Cdd:PRK14042  314 LDKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQAVINVLTG---------ERYKTITNEVKLYCQGKYGTPPGKISSAL 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  964 RSKVLKDLPRVEGRPGASLPPlDLQALEKELVDRhgeEVTPEDVLSAAMYPDVFAHFKDFTATFGPL-DSLNTRLFLQGP 1042
Cdd:PRK14042  385 RKKAIGRTEVIEVRPGDLLPN-ELDQLQNEISDL---ALSDEDVLLYAMFPEIGRQFLEQRKNNQLIpEPLLTQSSAPDN 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089 1043 KIAEEFEVELErGKTLHIKaLAVSDLNRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVID 1122
Cdd:PRK14042  461 SVMSEFDIILH-GESYHVK-VAGYGMIEHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIPGSIIA 538
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300538089 1123 IKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE 1178
Cdd:PRK14042  539 IHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
PRK14041 PRK14041
pyruvate carboxylase subunit B;
564-1053 1.70e-88

pyruvate carboxylase subunit B;


Pssm-ID: 237593 [Multi-domain]  Cd Length: 467  Bit Score: 294.00  E-value: 1.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  564 LLMDTTFRDAHQSLLATRVRTHDLKKIAPyvAHNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLL 643
Cdd:PRK14041    4 MFVDTTLRDGHQSLIATRMRTEDMLPALE--AFDRMGFYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQMLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  644 RGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLQYY 723
Cdd:PRK14041   82 RGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT---VSPVHT---LEYY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  724 MGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSG 803
Cdd:PRK14041  156 LEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPFSM 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  804 MTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGL 883
Cdd:PRK14041  235 GTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYD--VGMKSPDSRILVSQIPGGMYSNLVKQLKEQKM 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  884 GSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEaqaeelsfpRSVVEFLQGYIGVPHGGFPEPF 963
Cdd:PRK14041  313 LHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQAVLNVLTGERYKRVT---------NETKNYVKGLYGRPPAPIDEEL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  964 RSKVLKDLPRVEGRPGASLPPlDLQALEKELvdrhGEEV-TPEDVLSAAMYPDVfahfkdftatfgpldslnTRLFLQG- 1041
Cdd:PRK14041  384 MKKILGDEKPIDCRPADLLEP-ELEKARKEL----GILAeTDEDLLIYVILGEV------------------GKKFLKKk 440
                         490
                  ....*....|....*.
gi 300538089 1042 ----PKIAEEFEVELE 1053
Cdd:PRK14041  441 yeekIGVDFNLLEELS 456
PRK12330 PRK12330
methylmalonyl-CoA carboxytransferase subunit 5S;
571-1020 8.54e-81

methylmalonyl-CoA carboxytransferase subunit 5S;


Pssm-ID: 183445 [Multi-domain]  Cd Length: 499  Bit Score: 273.95  E-value: 8.54e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  571 RDAHQSLLATRVRTHDLKKIAPYVahNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVG 650
Cdd:PRK12330   13 RDAHQSLMATRMAMEDMVGACEDI--DNAGYWSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQMLLRGQNLLG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  651 YTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLQYYMGLAEEL 730
Cdd:PRK12330   91 YRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT---VSPIHT---VEGFVEQAKRL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  731 VRAGTHILCIKDMAGLLKPTACTMLVSSLRDRF-PDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMS-GMTSQP 808
Cdd:PRK12330  165 LDMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSMSlGPGHNP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  809 SMgALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAFDCTATmkSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFK 888
Cdd:PRK12330  245 TE-SLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTT--GVETEIFKSQIPGGMLSNMESQLKQQGAGDRMD 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  889 EVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlsraeaeaqaeelSFPRSVVEF---LQGYIGVPhggfPEPFRS 965
Cdd:PRK12330  322 EVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVFNVLMG-------------RYKVLTGEFadlMLGYYGET----PGERNP 384
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300538089  966 KVLKDLPR------VEGRPGASLPPlDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHF 1020
Cdd:PRK12330  385 EVVEQAKKqakkepITCRPADLLEP-EWDKLRAEALALEGCDGSDEDVLTYALFPQVAPKF 444
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
151-358 6.47e-78

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 254.92  E-value: 6.47e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   151 DKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGN 230
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   231 GALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTV 310
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 300538089   311 EFLVDRH-GKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSLP 358
Cdd:pfam02786  161 EFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
DRE_TIM_metallolyase cd03174
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ...
566-839 2.99e-69

DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163674 [Multi-domain]  Cd Length: 265  Bit Score: 233.12  E-value: 2.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  566 MDTTFRDAHQSLLATRvRTHDLKKIAPYVAHnfSKLFSMENWGGATFDVAmrFLYECPWRRLQELRELIPNIPFQMLLRG 645
Cdd:cd03174     1 TDTTLRDGLQSEGATF-STEDKLEIAEALDE--AGVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  646 anavgytnypdnvVFKFCEVAKENGMDVFRVFDSLNY--------------LPNMLLGMEAAGSAGGVVEAAISYTgdva 711
Cdd:cd03174    76 -------------REKGIERALEAGVDEVRIFDSASEthsrknlnksreedLENAEEAIEAAKEAGLEVEGSLEDA---- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  712 dpSRTKYSLQYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGA 791
Cdd:cd03174   139 --FGCKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGA 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 300538089  792 DVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWE 839
Cdd:cd03174   217 DRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
PRK12581 PRK12581
oxaloacetate decarboxylase; Provisional
565-1041 8.26e-66

oxaloacetate decarboxylase; Provisional


Pssm-ID: 79056 [Multi-domain]  Cd Length: 468  Bit Score: 230.39  E-value: 8.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  565 LMDTTFRDAHQSLLATRVRTHDLKKIAPYVahNFSKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 644
Cdd:PRK12581   15 ITETVLRDGHQSLMATRLSIEDMLPVLTIL--DKIGYYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNTRLQMLLR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  645 GANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvadpSRTKYSLQYYM 724
Cdd:PRK12581   93 GQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT------TSPVHTLNYYL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  725 GLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRdRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAADSMSGM 804
Cdd:PRK12581  167 SLVKELVEMGADSICIKDMAGILTPKAAKELVSGIK-AMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALSPFSEG 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  805 TSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEGARGLYAAfDCT--ATMKSGNSDVYENEIPGGQYTNLHFQAHSMG 882
Cdd:PRK12581  246 TSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYLA-DGIldPSLLFPDPRTLQYQVPGGMLSNMLSQLKQAN 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  883 LGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEaqaeelsfpRSVVEFLQGYIGVPHGGFPEP 962
Cdd:PRK12581  325 AESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVILGKPYQMVS---------KEIKQYLAGDYGKTPAPVNED 395
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300538089  963 FRSKVLKDLPRVEGRPGASLPPlDLQALEKELVDRhgeEVTPEDVLSAAMYPDVFAHFkdFTATFGPLDSLNTRLFLQG 1041
Cdd:PRK12581  396 LKRSQIGSAPVTTNRPADQLSP-EFEVLKAEVADL---AQTDEDVLTYALFPSVAKPF--LTTKYQTDDVIKVTAFIKA 468
Biotin_carb_N pfam00289
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ...
37-145 4.17e-57

Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.


Pssm-ID: 425585 [Multi-domain]  Cd Length: 108  Bit Score: 192.32  E-value: 4.17e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089    37 IKKVMVANRGEIAIRVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENNVDAVHP 116
Cdd:pfam00289    1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPG-PASESYLNIDAIIDAAKETGADAIHP 79
                           90       100
                   ....*....|....*....|....*....
gi 300538089   117 GYGFLSERADFAQACQDAGVRFIGPSPEV 145
Cdd:pfam00289   80 GYGFLSENAEFARACEEAGIIFIGPSPEA 108
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
98-355 1.87e-55

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 193.55  E-value: 1.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   98 HIPDIIKVAKE----NNVDAVHPGYGFLSERAdfAQACQDAGVRfiGPSPEVVRKMGDKVEARAIAIAAGVPVvPGTDaP 173
Cdd:COG0439     1 DIDAIIAAAAElareTGIDAVLSESEFAVETA--AELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFA-L 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  174 ITSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKpRHIEVQILGDQ 253
Cdd:COG0439    75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVRD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  254 yGNILHlyerdCSIQRRHQK---VVE---IAPAAhLDPQLRTRLTSDSVKLAKQVGYEN-AGTVEFLVDRHGKHYFIEVN 326
Cdd:COG0439   154 -GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYLIEIN 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 300538089  327 SRLQVEH--TVTEEITDVDLVHAQIHVAEGR 355
Cdd:COG0439   227 ARLGGEHipPLTELATGVDLVREQIRLALGE 257
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
375-482 2.86e-49

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 214878 [Multi-domain]  Cd Length: 107  Bit Score: 169.90  E-value: 2.86e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089    375 QCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRG 454
Cdd:smart00878    1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVD-SGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
                            90       100
                    ....*....|....*....|....*...
gi 300538089    455 VKTNIAFLQNVLNNQQFLAGTVDTQFID 482
Cdd:smart00878   80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
375-483 3.90e-43

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 426981 [Multi-domain]  Cd Length: 108  Bit Score: 152.26  E-value: 3.90e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   375 QCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRG 454
Cdd:pfam02785    1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVD-SGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
                           90       100
                   ....*....|....*....|....*....
gi 300538089   455 VKTNIAFLQNVLNNQQFLAGTVDTQFIDE 483
Cdd:pfam02785   80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
565-837 2.76e-27

HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.


Pssm-ID: 459902 [Multi-domain]  Cd Length: 264  Bit Score: 112.43  E-value: 2.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   565 LMDTTFRDAHQSLlATRVRTHDLKKIAPyvahnfsklfSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 644
Cdd:pfam00682    4 ICDTTLRDGEQAL-GVAFSIDEKLAIAR----------ALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCR 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   645 GAnavgytnypDNVVFKFCEVAKENGMDVFRVFDSLNYLP-NMLLGM---EAAGSAGGVVEAAISYTGDVA----DPSRT 716
Cdd:pfam00682   73 AR---------EHDIKAAVEALKGAGAVRVHVFIATSDLHrKYKLGKdreEVAKRAVAAVKAARSRGIDVEfspeDASRT 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   717 kySLQYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPD-LPLHIHTHDTSGAGVAAMLACAQAGADVVD 795
Cdd:pfam00682  144 --DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVD 221
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 300538089   796 VAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEY 837
Cdd:pfam00682  222 GTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANL 263
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
1111-1177 2.57e-24

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 97.10  E-value: 2.57e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300538089 1111 QIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEI 1177
Cdd:cd06850     1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
1111-1177 1.60e-18

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 80.72  E-value: 1.60e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300538089  1111 QIGAPMPGKVID-----IKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEI 1177
Cdd:pfam00364    2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
101-413 3.30e-14

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 77.70  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  101 DIIKVAKENNVDAVHPGYGflSERA-DFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDApiTSLHE 179
Cdd:PRK12815  621 DVLNVAEAENIKGVIVQFG--GQTAiNLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTA--TDEEE 696
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  180 AHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSealaafGNGALFVEKFIEKpRHIEVQILGDQY----- 254
Cdd:PRK12815  697 AFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENAS------QLYPILIDQFIDG-KEYEVDAISDGEdvtip 769
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  255 GNILHLYER-----DcSIQrrhqkvveIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDrHGKHYFIEVNSRl 329
Cdd:PRK12815  770 GIIEHIEQAgvhsgD-SIA--------VLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLA-NDEIYVLEVNPR- 838
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  330 qVEHTV--TEEITDVDLVHAQIHVAEGRSLPDLGLRQENIRINGcaiqcRVTTEDPARSFQ--PDTGRI---EVFRSGEG 402
Cdd:PRK12815  839 -ASRTVpfVSKATGVPLAKLATKVLLGKSLAELGYPNGLWPGSP-----FIHVKMPVFSYLkyPGVDNTlgpEMKSTGEV 912
                         330
                  ....*....|.
gi 300538089  403 MGIRLDNASAF 413
Cdd:PRK12815  913 MGIDKDLEEAL 923
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
128-419 3.94e-14

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 77.35  E-value: 3.94e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   128 AQACQDAGVRFIGPSPEVVrkmgDKVEARAIAIAA----GVPVVPGTDApiTSLHEAHEFSNTYGFPIIFKAAYGGGGRG 203
Cdd:TIGR01369  646 AKALEEAGVPILGTSPESI----DRAEDREKFSELldelGIPQPKWKTA--TSVEEAVEFASEIGYPVLVRPSYVLGGRA 719
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   204 MRVVHSYEELeenyTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQ-----YGNILHLyER------DCSIqrrhq 272
Cdd:TIGR01369  720 MEIVYNEEEL----RRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGeevliPGIMEHI-EEagvhsgDSTC----- 789
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   273 kvveIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDrHGKHYFIEVNSRlqVEHTV--TEEITDVDLVHAQIH 350
Cdd:TIGR01369  790 ----VLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVK-DGEVYVIEVNPR--ASRTVpfVSKATGVPLAKLAVR 862
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300538089   351 VAEGRSLPDLGLRQEniringcAIQCRVTTEDPARSFQPDTGR-----IEVFRSGEGMGIRLDNASAFQGAVIS 419
Cdd:TIGR01369  863 VMLGKKLEELGVGKE-------KEPKYVAVKEPVFSFSKLAGVdpvlgPEMKSTGEVMGIGRDLAEAFLKAQLS 929
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
35-329 4.59e-14

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 77.35  E-value: 4.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089    35 KPIKKVMVANRGEIAI-----------RVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLIgrglaPVQAYlHIPDII 103
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIgqaaefdysgsQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIE-----PLTPE-AVEKII 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   104 KvaKENnVDAVHPGYG---------FLSERAdfaqACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGtdAPI 174
Cdd:TIGR01369   78 E--KER-PDAILPTFGgqtalnlavELEESG----VLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   175 TSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRayseALAAFGNGALFVEKFIEKPRHIEVQILGDQY 254
Cdd:TIGR01369  149 HSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAER----ALSASPINQVLVEKSLAGWKEIEYEVMRDSN 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   255 GNILHLyerdCSIQR-----RH--QKVVeIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVD-RHGKHYFIEVN 326
Cdd:TIGR01369  225 DNCITV----CNMENfdpmgVHtgDSIV-VAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNpDSGRYYVIEVN 299

                   ...
gi 300538089   327 SRL 329
Cdd:TIGR01369  300 PRV 302
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
1110-1178 8.96e-14

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 69.54  E-value: 8.96e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300538089 1110 GQIGAPMPGKV-------IDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE 1178
Cdd:COG0511    61 GAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
128-328 6.64e-12

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 69.52  E-value: 6.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  128 AQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDApiTSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVV 207
Cdd:COG0458    91 EEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTA--TSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIV 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  208 HSYEELEEnytrAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNIL------HLyER------DcSIqrrhqkVV 275
Cdd:COG0458   169 YNEEELEE----YLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIivgimeHI-EPagvhsgD-SI------CV 236
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 300538089  276 eiAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDrHGKHYFIEVNSR 328
Cdd:COG0458   237 --APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD-DGRVYVIEVNPR 286
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
1112-1174 1.04e-11

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 63.29  E-value: 1.04e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300538089 1112 IGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLE-GDDLI 1174
Cdd:PRK06549   64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNpGDGLI 127
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
1110-1174 2.46e-11

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 62.96  E-value: 2.46e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300538089 1110 GQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLE-GDDLI 1174
Cdd:PRK05641   85 NVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDtGQPLI 150
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
151-326 3.17e-10

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 62.82  E-value: 3.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  151 DKVEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEALaAFGN 230
Cdd:COG1181    95 DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAA----ALEEAF-KYDD 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  231 GALfVEKFIEkPRHIEVQILGDQYGNILhlyerdcsiqrrhqKVVEIAPA--------------------AHLDPQLRTR 290
Cdd:COG1181   170 KVL-VEEFID-GREVTVGVLGNGGPRAL--------------PPIEIVPEngfydyeakytdggteyicpARLPEELEER 233
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 300538089  291 LTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVN 326
Cdd:COG1181   234 IQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVN 269
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
1111-1178 4.31e-10

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 56.72  E-value: 4.31e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300538089 1111 QIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTK-DMTLEGDDLiLEIE 1178
Cdd:PRK08225    3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEgDFVNEGDVL-LEIE 70
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
100-355 7.84e-10

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 61.50  E-value: 7.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  100 PDIIKVAKENNVDAVHPGYGFLSERADFAQACQDAGVRFIgPSPEVVRKMGDKVEARAIAIAAGVPVvpgtdaPIT---- 175
Cdd:COG0189    46 PELYRGEDLSEFDAVLPRIDPPFYGLALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPV------PPTlvtr 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  176 SLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEenytrAYSEALAAFGNGALFVEKFIEKPRHIEVQI--LGDQ 253
Cdd:COG0189   119 DPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALE-----SILEALTELGSEPVLVQEFIPEEDGRDIRVlvVGGE 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  254 YgniLHLYER-----DCSIQRRHQKVVEiapAAHLDPQLRTRLtsdsVKLAKQVGYENAGtVEFLVDRHGkHYFIEVNSR 328
Cdd:COG0189   194 P---VAAIRRipaegEFRTNLARGGRAE---PVELTDEERELA----LRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVT 261
                         250       260
                  ....*....|....*....|....*..
gi 300538089  329 LQVEHtvTEEITDVDLVHAQIHVAEGR 355
Cdd:COG0189   262 PGFRG--LERATGVDIAEAIADYLEAR 286
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
690-795 1.52e-09

3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163676  Cd Length: 274  Bit Score: 60.10  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  690 MEAAGSAGGVVEAAIS------YTGDVaDPSRTkyslqyyMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRF 763
Cdd:cd07938   120 AELAKAAGLRVRGYVStafgcpYEGEV-PPERV-------AEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERF 191
                          90       100       110
                  ....*....|....*....|....*....|..
gi 300538089  764 PDLPLHIHTHDTSGAGVAAMLACAQAGADVVD 795
Cdd:cd07938   192 PDEKLALHFHDTRGQALANILAALEAGVRRFD 223
LeuA COG0119
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ...
699-796 1.59e-07

Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439889 [Multi-domain]  Cd Length: 452  Bit Score: 55.17  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  699 VVEAAISYTGDVA----DPSRTkySLQYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHD 774
Cdd:COG0119   124 AVKYAKEHGLEVEfsaeDATRT--DPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHN 201
                          90       100
                  ....*....|....*....|..
gi 300538089  775 TSGAGVAAMLACAQAGADVVDV 796
Cdd:COG0119   202 DLGLAVANSLAAVEAGADQVEG 223
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
161-326 1.95e-07

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 52.70  E-value: 1.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   161 AAGVPVVP------GTDAPITSLHEAHEFSnTYGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEALAAfgNGALF 234
Cdd:pfam07478    4 AAGLPVVPfvtftrADWKLNPKEWCAQVEE-ALGYPVFVKPARLGSSVGVSKVESREELQA----AIEEAFQY--DEKVL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   235 VEKFIEKpRHIEVQILGDQYGNILHLYER--DCSIQRRHQK----VVEIAPAAHLDPQLRTRLTSDSVKLAKQVGYENAG 308
Cdd:pfam07478   77 VEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKyiddSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLA 155
                          170
                   ....*....|....*...
gi 300538089   309 TVEFLVDRHGKHYFIEVN 326
Cdd:pfam07478  156 RVDFFLTEDGEIVLNEVN 173
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
1111-1177 7.98e-07

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


Pssm-ID: 133456 [Multi-domain]  Cd Length: 73  Bit Score: 47.82  E-value: 7.98e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300538089 1111 QIGAPMP------GKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEI 1177
Cdd:cd06663     1 TILIPDLaqhlgdGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
78-328 1.04e-06

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 52.19  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   78 QKADEAYLIGRGLAPvqAYlhIPDIIKVAKENNVDAVHPGY----GFLSE-RADFaqacQDAGVRFIGPSPEVVRKMGDK 152
Cdd:PRK12767   41 YFADKFYVVPKVTDP--NY--IDRLLDICKKEKIDLLIPLIdpelPLLAQnRDRF----EEIGVKVLVSSKEVIEICNDK 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  153 VEARAIAIAAGVPVVPGTDAPITSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEenytRAYSEalaafgNGA 232
Cdd:PRK12767  113 WLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEY------VPN 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  233 LFVEKFIEkprHIE--VQILGDQYGNILHlyerdcSIQRRHQKVV-------EIAPAAHLDPQLRtrltsdsvKLAKQVG 303
Cdd:PRK12767  183 LIIQEFIE---GQEytVDVLCDLNGEVIS------IVPRKRIEVRagetskgVTVKDPELFKLAE--------RLAEALG 245
                         250       260
                  ....*....|....*....|....*
gi 300538089  304 YENAGTVEFLVdRHGKHYFIEVNSR 328
Cdd:PRK12767  246 ARGPLNIQCFV-TDGEPYLFEINPR 269
carB PRK05294
carbamoyl-phosphate synthase large subunit;
128-368 1.12e-06

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 53.18  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  128 AQACQDAGVRFIGPSPEVVrkmgDKVEAR----AIAIAAGVPVVPGTDApiTSLHEAHEFSNTYGFPIIFKAAYGGGGRG 203
Cdd:PRK05294  646 AKALEAAGVPILGTSPDAI----DLAEDRerfsKLLEKLGIPQPPNGTA--TSVEEALEVAEEIGYPVLVRPSYVLGGRA 719
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  204 MRVVHSYEELEEnYTRaysEALAAFGNGALFVEKFIEKPRHIEVQILGD----QYGNIL-HLyER------D--CSIqrr 270
Cdd:PRK05294  720 MEIVYDEEELER-YMR---EAVKVSPDHPVLIDKFLEGAIEVDVDAICDgedvLIGGIMeHI-EEagvhsgDsaCSL--- 791
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  271 hqkvveiaPAAHLDPQLRTRLTSDSVKLAKQ---VGYENagtVEFLVdRHGKHYFIEVN---SRlqvehTV--TEEITDV 342
Cdd:PRK05294  792 --------PPQTLSEEIIEEIREYTKKLALElnvVGLMN---VQFAV-KDDEVYVIEVNpraSR-----TVpfVSKATGV 854
                         250       260
                  ....*....|....*....|....*.
gi 300538089  343 DLVHAQIHVAEGRSLPDLGLRQENIR 368
Cdd:PRK05294  855 PLAKIAARVMLGKKLAELGYTKGLIP 880
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
135-329 3.48e-06

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 51.51  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  135 GVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVvPGTDApITSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELE 214
Cdd:PRK12815  112 GVELLGTNIEAIQKGEDRERFRALMKELGEPV-PESEI-VTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELE 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  215 ENYTRAysEALAAFGNgaLFVEKFIEKPRHIEVQILGDQYGNILHLyerdCSIQRrhqkvVE-----------IAPAAHL 283
Cdd:PRK12815  190 QLFKQG--LQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCITV----CNMEN-----IDpvgihtgdsivVAPSQTL 256
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 300538089  284 DPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYF-IEVNSRL 329
Cdd:PRK12815  257 TDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYlIEVNPRV 303
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
141-324 6.78e-06

Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439797 [Multi-domain]  Cd Length: 353  Bit Score: 49.69  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  141 PSPEVVRKMGDKVEARAIAIAAGVPVVPGtdAPITSLHEAHEFSNTYGFPIIFKAAyggggrgmR---------VVHSYE 211
Cdd:COG0026    79 PGPEALEIAQDRLLEKAFLAELGIPVAPF--AAVDSLEDLEAAIAELGLPAVLKTR--------RggydgkgqvVIKSAA 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  212 ELEenytraysEALAAFGNGALFVEKFI--EKprhiEVQILG--DQYGNILHlY---ErdcSIQRRHQKVVEIAPaAHLD 284
Cdd:COG0026   149 DLE--------AAWAALGGGPCILEEFVpfER----ELSVIVarSPDGEVAT-YpvvE---NVHRNGILDESIAP-ARIS 211
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300538089  285 PQLRTRLTSDSVKLAKQVGYenAGT--VEFLVDRHGK--------------HYFIE 324
Cdd:COG0026   212 EALAAEAEEIAKRIAEALDY--VGVlaVEFFVTKDGEllvneiaprphnsgHWTIE 265
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
1111-1177 1.15e-05

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 44.29  E-value: 1.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300538089 1111 QIGAPM-PGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEI 1177
Cdd:COG0508     9 DLGESMtEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
PRK09389 PRK09389
(R)-citramalate synthase; Provisional
712-796 1.27e-05

(R)-citramalate synthase; Provisional


Pssm-ID: 236493 [Multi-domain]  Cd Length: 488  Bit Score: 49.17  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  712 DPSRTkySLQYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRfPDLPLHIHTHDTSGAGVAAMLACAQAGA 791
Cdd:PRK09389  136 DASRA--DLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSEL-VKGPVSIHCHNDFGLAVANTLAALAAGA 212

                  ....*
gi 300538089  792 DVVDV 796
Cdd:PRK09389  213 DQVHV 217
PRK14573 PRK14573
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
138-326 2.35e-05

bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;


Pssm-ID: 184752 [Multi-domain]  Cd Length: 809  Bit Score: 48.66  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  138 FIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTdaPITsLHE--------AHEFSNTYGFPIIFKAAYGGGGRGMRVVHS 209
Cdd:PRK14573  555 YTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQ--PLT-LAGwkrepelcLAHIVEAFSFPMFVKTAHLGSSIGVFEVHN 631
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  210 YEELEEnytrAYSEALAAfgNGALFVEKFIEKPRHIEVQILGDQYGN--ILHLYERdC------SIQRRH----QKVVEI 277
Cdd:PRK14573  632 VEELRD----KISEAFLY--DTDVFVEESRLGSREIEVSCLGDGSSAyvIAGPHER-RgsggfiDYQEKYglsgKSSAQI 704
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300538089  278 APAAHLDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVN 326
Cdd:PRK14573  705 VFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMN 753
DRE_TIM_IPMS cd07940
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ...
700-796 4.74e-05

2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163678  Cd Length: 268  Bit Score: 46.67  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  700 VEAAISYTGDVA----DPSRTkySLQYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFP--DLPLHIHTH 773
Cdd:cd07940   120 VEYAKSHGLDVEfsaeDATRT--DLDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPniKVPISVHCH 197
                          90       100
                  ....*....|....*....|...
gi 300538089  774 DTSGAGVAAMLACAQAGADVVDV 796
Cdd:cd07940   198 NDLGLAVANSLAAVEAGARQVEC 220
DRE_TIM_HOA cd07943
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ...
723-804 4.79e-05

4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF ) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163681  Cd Length: 263  Bit Score: 46.34  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  723 YMGLAEELVR-------AGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVD 795
Cdd:cd07943   136 HMASPEELAEqaklmesYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRID 215

                  ....*....
gi 300538089  796 VaadSMSGM 804
Cdd:cd07943   216 G---SLAGL 221
PRK05889 PRK05889
biotin/lipoyl-binding carrier protein;
1114-1177 1.08e-04

biotin/lipoyl-binding carrier protein;


Pssm-ID: 180306 [Multi-domain]  Cd Length: 71  Bit Score: 41.72  E-value: 1.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300538089 1114 APMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEI 1177
Cdd:PRK05889    7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
151-326 1.12e-04

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 45.49  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  151 DKVEARAIAIAAGVPVVPGT--DAPITSLHEAHEFsntyGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEAlAAF 228
Cdd:PRK01372   98 DKLRTKLVWQAAGLPTPPWIvlTREEDLLAAIDKL----GLPLVVKPAREGSSVGVSKVKEEDELQA----ALELA-FKY 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  229 GNGALfVEKFIeKPRHIEVQILGDQygnILhlyerdcsiqrrhqKVVEIAPAAH--------------------LDPQLR 288
Cdd:PRK01372  169 DDEVL-VEKYI-KGRELTVAVLGGK---AL--------------PVIEIVPAGEfydyeakylaggtqyicpagLPAEIE 229
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 300538089  289 TRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVN 326
Cdd:PRK01372  230 AELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVN 267
PLN02735 PLN02735
carbamoyl-phosphate synthase
136-419 1.35e-04

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 46.31  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  136 VRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDApiTSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEe 215
Cdd:PLN02735  687 VKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIA--RSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK- 763
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  216 nytRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNI-------------LHLYERDCSIqrrhqkvveiaPAAH 282
Cdd:PLN02735  764 ---TYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVviggimehieqagVHSGDSACSL-----------PTQT 829
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  283 LDPQLRTRLTSDSVKLAKQVGYENAGTVEFLVDRHGKHYFIEVNSRlqVEHT---VTEEITDVDLVHAQIhVAEGRSLPD 359
Cdd:PLN02735  830 IPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR--ASRTvpfVSKAIGHPLAKYASL-VMSGKSLKD 906
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300538089  360 LGLRQENIrINGCAIQCRVTtedPARSFQ-PDTGRIEVFRS-GEGMGIRLDNASAFQGAVIS 419
Cdd:PLN02735  907 LGFTEEVI-PAHVSVKEAVL---PFDKFQgCDVLLGPEMRStGEVMGIDYEFSKAFAKAQIA 964
PLN02735 PLN02735
carbamoyl-phosphate synthase
19-329 3.54e-04

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 44.77  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   19 TSTAPAASPNVRRLeyKPIKKVMVANRGEIAI-----------RVFRACTELGIRTVAIYSEQDTGQMHRQKADEAYLig 87
Cdd:PLN02735    7 VTRAWSAATKAGKR--TDLKKIMILGAGPIVIgqacefdysgtQACKALKEEGYEVVLINSNPATIMTDPETADRTYI-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   88 rglAPVQaylhiPDII-KVAKENNVDAVHPGYG---------FLSERADFAQAcqdaGVRFIGPSPEVVRKMGDKVEARA 157
Cdd:PLN02735   83 ---APMT-----PELVeQVIAKERPDALLPTMGgqtalnlavALAESGILEKY----GVELIGAKLDAIKKAEDRELFKQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  158 IAIAAGVPVVPGTDApiTSLHEAHEFSNTYG-FPIIFKAAYGGGGRGMRVVHSYEELEENYTraysEALAAFGNGALFVE 236
Cdd:PLN02735  151 AMEKIGLKTPPSGIA--TTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICK----AGLAASITSQVLVE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  237 KFIEKPRHIEVQILGDQYGNILHLyerdCSIQRRHQKVVE------IAPAAHLDPQLRTRLTSDSVKLAKQVGYENAGT- 309
Cdd:PLN02735  225 KSLLGWKEYELEVMRDLADNVVII----CSIENIDPMGVHtgdsitVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSn 300
                         330       340
                  ....*....|....*....|.
gi 300538089  310 VEFLVD-RHGKHYFIEVNSRL 329
Cdd:PLN02735  301 VQFAVNpVDGEVMIIEMNPRV 321
aksA PRK11858
trans-homoaconitate synthase; Reviewed
712-796 6.53e-04

trans-homoaconitate synthase; Reviewed


Pssm-ID: 183341 [Multi-domain]  Cd Length: 378  Bit Score: 43.62  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  712 DPSRTKYS-LQYYMGLAEElvrAGTHILCIKDMAGLLKPTACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAG 790
Cdd:PRK11858  138 DASRTDLDfLIEFAKAAEE---AGADRVRFCDTVGILDPFTMYELVKELVEAV-DIPIEVHCHNDFGMATANALAGIEAG 213

                  ....*.
gi 300538089  791 ADVVDV 796
Cdd:PRK11858  214 AKQVHT 219
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
1112-1178 6.54e-04

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 43.71  E-value: 6.54e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300538089  1112 IGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE 1178
Cdd:TIGR01348    8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
PRK02186 PRK02186
argininosuccinate lyase; Provisional
72-363 8.85e-04

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 43.68  E-value: 8.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   72 TGQMHRQKA----DEAYLI--GRGLAPVQAYLHIPDIikVAKENNVDAVHpgyGFLSERADFA--QACQDAgvrFIGPSP 143
Cdd:PRK02186   15 TGELLLRKAllrgFTPYFLtaNRGKYPFLDAIRVVTI--SADTSDPDRIH---RFVSSLDGVAgiMSSSEY---FIEVAS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  144 EVVRKMG-DKVEARAIAIA------------AGVPVvPGTDApITSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSY 210
Cdd:PRK02186   87 EVARRLGlPAANTEAIRTCrdkkrlartlrdHGIDV-PRTHA-LALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  211 EELEenytrAYSEALAAFGNGALFVEKFIEKPRHiEVQILGDQYGniLHLyerdCSIQRRHQ----KVVEIA---PAAHL 283
Cdd:PRK02186  165 AEAA-----AHCAALRRAGTRAALVQAYVEGDEY-SVETLTVARG--HQV----LGITRKHLgpppHFVEIGhdfPAPLS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  284 DPQlRTRLTSDSVKLAKQVGYE-NAGTVEFLVdRHGKHYFIEVNSRLQ--VEHTVTEEITDVDLVHAQIHVAEGRSlPDL 360
Cdd:PRK02186  233 APQ-RERIVRTVLRALDAVGYAfGPAHTELRV-RGDTVVIIEINPRLAggMIPVLLEEAFGVDLLDHVIDLHLGVA-AFA 309

                  ...
gi 300538089  361 GLR 363
Cdd:PRK02186  310 DPT 312
carB PRK05294
carbamoyl-phosphate synthase large subunit;
37-328 8.85e-04

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 43.55  E-value: 8.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089   37 IKKVMVANRGEI--------------AIRVFRactELGIRTVAIYSEQDTGQMHRQKADEAYLIgrglaPVQaylhiPDI 102
Cdd:PRK05294    7 IKKILIIGSGPIvigqacefdysgtqACKALR---EEGYRVVLVNSNPATIMTDPEMADATYIE-----PIT-----PEF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  103 I-KVAKENNVDAVHPGYG---------------FLSERadfaqacqdaGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPV 166
Cdd:PRK05294   74 VeKIIEKERPDAILPTMGgqtalnlavelaesgVLEKY----------GVELIGAKLEAIDKAEDRELFKEAMKKIGLPV 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  167 VPGTdaPITSLHEAHEFSNTYGFPIIFKAAYGgggrgM-----RVVHSYEELEENYTRayseALAAFGNGALFVEKFIEK 241
Cdd:PRK05294  144 PRSG--IAHSMEEALEVAEEIGYPVIIRPSFT-----LggtggGIAYNEEELEEIVER----GLDLSPVTEVLIEESLLG 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  242 PRHIEVQILGDQYGN--ILhlyerdCSIqrrhqkvvE--------------IAPAAHLDPQLRTRLTSDSVKLAKQVGYE 305
Cdd:PRK05294  213 WKEYEYEVMRDKNDNciIV------CSI--------EnidpmgvhtgdsitVAPAQTLTDKEYQMLRDASIAIIREIGVE 278
                         330       340
                  ....*....|....*....|....*
gi 300538089  306 NAGT-VEFLVDRH-GKHYFIEVNSR 328
Cdd:PRK05294  279 TGGCnVQFALNPKdGRYIVIEMNPR 303
DRE_TIM_LeuA3 cd07941
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ...
756-794 9.45e-04

Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel domain; Desulfobacterium autotrophicum LeuA3 is sequence-similar to alpha-isopropylmalate synthase (LeuA) but its exact function is unknown. Members of this family have an N-terminal TIM barrel domain that belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163679  Cd Length: 273  Bit Score: 42.44  E-value: 9.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 300538089  756 VSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVV 794
Cdd:cd07941   186 VKEVRERLPGVPLGIHAHNDSGLAVANSLAAVEAGATQV 224
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
1118-1178 1.98e-03

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 42.30  E-value: 1.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300538089 1118 GKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE 1178
Cdd:PRK11854   15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
DRE_TIM_CMS cd07945
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ...
717-839 3.12e-03

Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic TIM barrel domain; Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step of the citramalate pathway. Citramalate is only found in Leptospira interrogans and a few other microorganisms. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163683 [Multi-domain]  Cd Length: 280  Bit Score: 40.82  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  717 KYSLQYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDV 796
Cdd:cd07945   143 RDSPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVLAAVKAGIKGLHT 222
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 300538089  797 AADSMSGMTSQPSMGALVACTRG-TPLDTEVPMERVFDYSEYWE 839
Cdd:cd07945   223 TVNGLGERAGNAPLASVIAVLKDkLKVKTNIDEKRLNRASRLVE 266
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
1105-1178 4.15e-03

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 41.01  E-value: 4.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300538089  1105 LKDVK-GQIGAPMPGKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE 1178
Cdd:TIGR01348  116 VQEVTvPDIGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
1104-1178 4.19e-03

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 41.14  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089 1104 ALKDVKgqigapMP------GKVIDIKVVAGAKVAKGQPLCVLSAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEI 1177
Cdd:PRK11854  205 GVKDVN------VPdiggdeVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF 278

                  .
gi 300538089 1178 E 1178
Cdd:PRK11854  279 E 279
DRE_TIM_NifV cd07939
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ...
699-796 6.53e-03

Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163677 [Multi-domain]  Cd Length: 259  Bit Score: 39.80  E-value: 6.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300538089  699 VVEAAISYTGDVA----DPSRTKYS-LQYYMGLAEElvrAGTHILCIKDMAGLLKPTACTMLVSSLRDRFpDLPLHIHTH 773
Cdd:cd07939   115 LVGRAKDRGLFVSvgaeDASRADPDfLIEFAEVAQE---AGADRLRFADTVGILDPFTTYELIRRLRAAT-DLPLEFHAH 190
                          90       100
                  ....*....|....*....|...
gi 300538089  774 DTSGAGVAAMLACAQAGADVVDV 796
Cdd:cd07939   191 NDLGLATANTLAAVRAGATHVSV 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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