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Conserved domains on  [gi|2039176577|emb|CAG6061214|]
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chorismate binding enzyme para-aminobenzoate synthetase [Streptococcus pneumoniae]

Protein Classification

bifunctional aminodeoxychorismate synthase component I/class IV aminotransferase( domain architecture ID 10015691)

bifunctional aminodeoxychorismate synthase component I/class IV aminotransferase is a pyridoxaL 5'-phosphate dependent enzyme (PLPDE)

EC:  2.6.1.85
Gene Ontology:  GO:0030170|GO:0046820
PubMed:  31989227|11450855

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pabB TIGR00553
aminodeoxychorismate synthase, component I, bacterial clade; Members of this family, ...
 50-368 0e+00

aminodeoxychorismate synthase, component I, bacterial clade; Members of this family, aminodeoxychorismate synthase, component I (PabB), were designated para-aminobenzoate synthase component I until it was recognized that PabC, a lyase, completes the pathway of PABA synthesis. This family is closely related to anthranilate synthase component I (trpE), and both act on chorismate. The clade of PabB enzymes represented by this model includes sequences from Gram-positive and alpha and gamma Proteobacteria as well as Chlorobium, Nostoc, Fusobacterium and Arabidopsis. A closely related clade of fungal PabB enzymes is identified by TIGR01823, while another bacterial clade of potential PabB enzymes is more closely related to TrpE (TIGR01824). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


:

Pssm-ID: 273133  Cd Length: 328  Bit Score: 520.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  50 VVGYVSYEAAP--AFEEKLAVHKDPLLGEYLLYFTVHDSVETSPIPLTYEDIDLPSNWQEVTSA-------ADYEKAIAQ 120
Cdd:TIGR00553   1 LVGYLSYEAGPdaAFEPYDAALLADHRRTPLLRFLVFERVEAQPRAAVEAEDDAPADRQAPTSDiqsemtrAEYGEAIDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 121 IHHHLRQGDTYQVNYTVQLKQKLSANPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELFFEQNDRELTTRPMKGTTQR 200
Cdd:TIGR00553  81 LQDYIRAGDCYQANLTQQFHATWDGDPLAAFRKLRRRQPAPFSAFLDLGDGAILSLSPELFFSIDGSEIETRPIKGTLPR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 201 GVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFR 280
Cdd:TIGR00553 161 GADPQEDRAQASALAESAKDRAENLMIVDLLRNDLGRIAEVGSVKVPELFVVETYPTVHQLVSTITARLREDLTLSDLFR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 281 SLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGITWDSTWESEYRE 360
Cdd:TIGR00553 241 ALFPGGSITGAPKVRAMEIIDELEPQPRGVYCGAIGYLSPEGDMDFNVAIRTLTLDGGRAVYGVGGGIVADSDPEAEYRE 320


                  ....*...
gi 2039176577 361 VHQKAAVL 368
Cdd:TIGR00553 321 CLLKAAPL 328
PLPDE_IV super family cl00224
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 375-570 7.14e-33

PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.


The actual alignment was detected with superfamily member PRK07546:

Pssm-ID: 444764 [Multi-domain]  Cd Length: 209  Bit Score: 125.09  E-value: 7.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 375 FQLITTgeisqknLLFE--------DQHLERLRKASRYFAFPFDAEDLGHKIEEECQDCEANQdyRLRISLSKSGEIEVN 446
Cdd:PRK07546    4 FELIET-------LRWEpgagfprlDRHLARLERSARALGFPCDPAAVRAKLAEAVAGAQGPL--RLRLTLARDGRLTVE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 447 RQVLTPLSTSfCQAQVCLQEAALNQS--FTYFKTTHRP--------HLSLGEQEKIYHNKSGELLETSIGNLVLKIAGKL 516
Cdd:PRK07546   75 TAPLPPLPPD-TVWRVAIARTRLDSAdpLLRYKTTRRAaydaaraeLPPAEADEVILLNERGEVCEGTITNVFLDRGGGM 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2039176577 517 Y-TPPIRLGILPGIYRQHLLETGQVEEKVLTLADLTQAEAIYGCNAVRGLYELSL 570
Cdd:PRK07546  154 LtTPPLSCGLLPGVLRAELLDAGRAREAVLTVDDLKSARAIWVGNSLRGLIRAEL 208
 
Name Accession Description Interval E-value
pabB TIGR00553
aminodeoxychorismate synthase, component I, bacterial clade; Members of this family, ...
 50-368 0e+00

aminodeoxychorismate synthase, component I, bacterial clade; Members of this family, aminodeoxychorismate synthase, component I (PabB), were designated para-aminobenzoate synthase component I until it was recognized that PabC, a lyase, completes the pathway of PABA synthesis. This family is closely related to anthranilate synthase component I (trpE), and both act on chorismate. The clade of PabB enzymes represented by this model includes sequences from Gram-positive and alpha and gamma Proteobacteria as well as Chlorobium, Nostoc, Fusobacterium and Arabidopsis. A closely related clade of fungal PabB enzymes is identified by TIGR01823, while another bacterial clade of potential PabB enzymes is more closely related to TrpE (TIGR01824). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 273133  Cd Length: 328  Bit Score: 520.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  50 VVGYVSYEAAP--AFEEKLAVHKDPLLGEYLLYFTVHDSVETSPIPLTYEDIDLPSNWQEVTSA-------ADYEKAIAQ 120
Cdd:TIGR00553   1 LVGYLSYEAGPdaAFEPYDAALLADHRRTPLLRFLVFERVEAQPRAAVEAEDDAPADRQAPTSDiqsemtrAEYGEAIDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 121 IHHHLRQGDTYQVNYTVQLKQKLSANPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELFFEQNDRELTTRPMKGTTQR 200
Cdd:TIGR00553  81 LQDYIRAGDCYQANLTQQFHATWDGDPLAAFRKLRRRQPAPFSAFLDLGDGAILSLSPELFFSIDGSEIETRPIKGTLPR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 201 GVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFR 280
Cdd:TIGR00553 161 GADPQEDRAQASALAESAKDRAENLMIVDLLRNDLGRIAEVGSVKVPELFVVETYPTVHQLVSTITARLREDLTLSDLFR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 281 SLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGITWDSTWESEYRE 360
Cdd:TIGR00553 241 ALFPGGSITGAPKVRAMEIIDELEPQPRGVYCGAIGYLSPEGDMDFNVAIRTLTLDGGRAVYGVGGGIVADSDPEAEYRE 320


                  ....*...
gi 2039176577 361 VHQKAAVL 368
Cdd:TIGR00553 321 CLLKAAPL 328
PRK07508 PRK07508
aminodeoxychorismate synthase component I;
8-365 6.94e-133

aminodeoxychorismate synthase component I;


Pssm-ID: 236035 [Multi-domain]  Cd Length: 378  Bit Score: 392.45  E-value: 6.94e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577   8 DFRTLGERYTFTQPIKELKTRNVEEVADLLAQVESYQEQGYYVVGYVSYEAAPAFEEKLAvhkdPLLGEY----LLYFTV 83
Cdd:PRK07508    6 RDDPAGRAVLFADPSEIIRARTPDEFAPALAAMERARAAGKWLAGYLSYEAGYLLEPKLA----PLMPEGretpLLCFGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  84 HDS-VETSPIPLTYED-----IDLPSNWqevtSAADYEKAIAQIHHHLRQGDTYQVNYTVQLKQKLSANPFAIYNRMVVE 157
Cdd:PRK07508   82 FDApSPEAPAPARPSEnaarlRDPVARW----DFADYAQRFERLHRHIRAGDCYQANLTFPLDARWGGDPLALFWALAAR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 158 QEAGYNAYVEHDEMAVISMSPELFFE-QNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMN 236
Cdd:PRK07508  158 QPVGYGALVDLGGPVILSRSPELFFRvDGEGWIETHPMKGTAPRGATPAEDARLRAALLNDEKNQAENRMIVDLLRNDIS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 237 RISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIG 316
Cdd:PRK07508  238 RISEVGSLDVPELFDIETYPTVHQMVSRVRARLLPGLGLADIFAALFPCGSITGAPKIRAMEILRELEPGPRDLYCGAIG 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2039176577 317 LLLPNGRRIFNVAIRTIQLHK-GQAIYGVGGGITWDSTWESEYREVHQKA 365
Cdd:PRK07508  318 WIAPDGRMRFNVAIRTLSLFPgGRAVFNVGGGIVFDSTAEAEYEECLLKA 367
Chorismate_bind pfam00425
chorismate binding enzyme; This family includes the catalytic regions of the chorismate ...
 112-364 3.32e-113

chorismate binding enzyme; This family includes the catalytic regions of the chorismate binding enzymes anthranilate synthase, isochorismate synthase, aminodeoxychorismate synthase and para-aminobenzoate synthase.


Pssm-ID: 425674 [Multi-domain]  Cd Length: 255  Bit Score: 337.22  E-value: 3.32e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 112 ADYEKAIAQIHHHLRQGDTYQVNYTVQLKQKL--SANPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELFFEQNDREL 189
Cdd:pfam00425   1 EDYLAAVEKAKEAIRAGDLYKVVLSRRLTLPLagDIDPLALYRRLRARNPAPYSFYFRTGDFTFLGASPERLLSVDGGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 190 TTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQL 269
Cdd:pfam00425  81 ITEPIAGTRPRGKDPAEDEALAAELLADPKERAEHLMVVDLIRNDLGRVCVPGSVKVPELPEVERYGTVQHLVSTISGRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 270 REDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGIT 349
Cdd:pfam00425 161 KPGLSLLDLLKALFPTGAVTGAPKKRAMEIIRELEPFPRGLYAGAVGYLDPDGDADFAVAIRTALVDNGRARLYAGAGIV 240

                         250
                  ....*....|....*
gi 2039176577 350 WDSTWESEYREVHQK 364
Cdd:pfam00425 241 ADSDPEAEWEETEAK 255
TrpE COG0147
Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism, ...
 51-368 4.55e-109

Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthases component I is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439917 [Multi-domain]  Cd Length: 416  Bit Score: 332.84  E-value: 4.55e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  51 VGYVSYEAAPAFEEKLAVHKDPLlGEYLLYFTVHDSVetspipLTYediDLPSNWQEVTSAADYEKAIAQIHHHLRQGDT 130
Cdd:COG0147   103 VGYFGYDLVRYFERLPDLAPDDL-GLPDAALGLYDRL------LVF---DHLKGTRSNFTREEYLAAVERAKEYIRAGDI 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 131 YQVNYTVQLKQKLSANPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQ 210
Cdd:COG0147   173 FQVVLSQRFSAPFEGDPLALYRALRRINPSPYMFYLRFGDFAIVGSSPERLVRVEDGRVETRPIAGTRPRGATPEEDAAL 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 211 ASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITG 290
Cdd:COG0147   253 AEELLADEKERAEHLMLVDLARNDLGRVCEPGSVKVPELMVVERYSHVMHLVSTVTGRLRPGLDALDALRATFPAGTLTG 332

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2039176577 291 APKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGITWDSTWESEYREVHQKAAVL 368
Cdd:COG0147   333 APKIRAMEIIDELEPTRRGVYGGAVGYLSFDGNMDLAIAIRTAVVKDGRAYVQAGAGIVADSDPEAEYQETLNKARAL 410
PRK07546 PRK07546
hypothetical protein; Provisional
 375-570 7.14e-33

hypothetical protein; Provisional


Pssm-ID: 169002 [Multi-domain]  Cd Length: 209  Bit Score: 125.09  E-value: 7.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 375 FQLITTgeisqknLLFE--------DQHLERLRKASRYFAFPFDAEDLGHKIEEECQDCEANQdyRLRISLSKSGEIEVN 446
Cdd:PRK07546    4 FELIET-------LRWEpgagfprlDRHLARLERSARALGFPCDPAAVRAKLAEAVAGAQGPL--RLRLTLARDGRLTVE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 447 RQVLTPLSTSfCQAQVCLQEAALNQS--FTYFKTTHRP--------HLSLGEQEKIYHNKSGELLETSIGNLVLKIAGKL 516
Cdd:PRK07546   75 TAPLPPLPPD-TVWRVAIARTRLDSAdpLLRYKTTRRAaydaaraeLPPAEADEVILLNERGEVCEGTITNVFLDRGGGM 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2039176577 517 Y-TPPIRLGILPGIYRQHLLETGQVEEKVLTLADLTQAEAIYGCNAVRGLYELSL 570
Cdd:PRK07546  154 LtTPPLSCGLLPGVLRAELLDAGRAREAVLTVDDLKSARAIWVGNSLRGLIRAEL 208
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 376-566 2.36e-31

Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 121.31  E-value: 2.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 376 QLITTGEISQKNLLFEDQHLERLRKASRYFA--FPFDAEDLGHKIEEeCQDCEANQDYRLRISLSKSGE------IEVNR 447
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGipLPFDEEDLRKIIEE-LLKANGLGVGRLRLTVSRGPGgfglptSDPTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 448 QV----LTPLSTSFCQA-QVCLQEAALNQSFTYFKTTHRP--------HLSLGEQEKIYHNKSGELLETSIGNLVLKIAG 514
Cdd:pfam01063  80 AIfvsaLPPPPESKKKGvISSLVRRNPPSPLPGAKTLNYLenvlarreAKAQGADDALLLDEDGNVTEGSTSNVFLVKGG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2039176577 515 KLYTPPIRLGILPGIYRQHLLETGQ-----VEEKVLTLADLTQAEAIYGCNAVRGLY 566
Cdd:pfam01063 160 TLYTPPLESGILPGITRQALLDLAKalgleVEERPITLADLQEADEAFLTNSLRGVT 216
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 377-565 4.25e-16

ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.


Pssm-ID: 238800 [Multi-domain]  Cd Length: 249  Bit Score: 78.12  E-value: 4.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 377 LITTGEISQKNLLFEDQHLERLRKASRYFAFPFDAEDlghKIEEECQDCEANQDY---RLRISLS-----KSGEIEVNR- 447
Cdd:cd01559    10 VFETMRALDGRLFLLDAHLARLERSARRLGIPEPDLP---RLRAALESLLAANDIdegRIRLILSrgpggRGYAPSVCPg 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 448 ----QVLTPLSTSFCQAQV----CLQEAALNQSFTYFKTTHR--PHLSL------GEQEKIYHNKSGELLETSIGNLVLK 511
Cdd:cd01559    87 palyVSVIPLPPAWRQDGVrlitCPVRLGEQPLLAGLKHLNYleNVLAKreardrGADEALFLDTDGRVIEGTASNLFFV 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2039176577 512 IAGKLYTPPIRLGILPGIYRQHLLETG-----QVEEKVLTLADLTQAEAIYGCNAVRGL 565
Cdd:cd01559   167 KDGELVTPSLDRGGLAGITRQRVIELAaakgyAVDERPLRLEDLLAADEAFLTNSLLGV 225
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 388-565 4.31e-16

Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439885 [Multi-domain]  Cd Length: 285  Bit Score: 78.69  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 388 LLFEDQHLERLRKASR--YFAFPFDAEDLghkiEEECQD-CEAN--QDYRLRISLS--------KSGEIEVNRQVLT-PL 453
Cdd:COG0115    41 LFRLDEHLARLNRSAKrlGIPIPYTEEEL----LEAIRElVAANglEDGYIRPQVTrgvggrgvFAEEYEPTVIIIAsPL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 454 STSFCQAQ-------VCLQEAALNQSFTYFKTTHRPHLSLGEQEK--------IYHNKSGELLETSIGNLVLKIAGKLYT 518
Cdd:COG0115   117 PAYPAEAYekgvrviTSPYRRAAPGGLGGIKTGNYLNNVLAKQEAkeagadeaLLLDTDGYVAEGSGSNVFIVKDGVLVT 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2039176577 519 PPIRLGILPGIYRQHLLE----TG-QVEEKVLTLADLTQAEAIYGCNAVRGL 565
Cdd:COG0115   197 PPLSGGILPGITRDSVIElareLGiPVEERPISLEELYTADEVFLTGTAAEV 248
 
Name Accession Description Interval E-value
pabB TIGR00553
aminodeoxychorismate synthase, component I, bacterial clade; Members of this family, ...
 50-368 0e+00

aminodeoxychorismate synthase, component I, bacterial clade; Members of this family, aminodeoxychorismate synthase, component I (PabB), were designated para-aminobenzoate synthase component I until it was recognized that PabC, a lyase, completes the pathway of PABA synthesis. This family is closely related to anthranilate synthase component I (trpE), and both act on chorismate. The clade of PabB enzymes represented by this model includes sequences from Gram-positive and alpha and gamma Proteobacteria as well as Chlorobium, Nostoc, Fusobacterium and Arabidopsis. A closely related clade of fungal PabB enzymes is identified by TIGR01823, while another bacterial clade of potential PabB enzymes is more closely related to TrpE (TIGR01824). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 273133  Cd Length: 328  Bit Score: 520.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  50 VVGYVSYEAAP--AFEEKLAVHKDPLLGEYLLYFTVHDSVETSPIPLTYEDIDLPSNWQEVTSA-------ADYEKAIAQ 120
Cdd:TIGR00553   1 LVGYLSYEAGPdaAFEPYDAALLADHRRTPLLRFLVFERVEAQPRAAVEAEDDAPADRQAPTSDiqsemtrAEYGEAIDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 121 IHHHLRQGDTYQVNYTVQLKQKLSANPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELFFEQNDRELTTRPMKGTTQR 200
Cdd:TIGR00553  81 LQDYIRAGDCYQANLTQQFHATWDGDPLAAFRKLRRRQPAPFSAFLDLGDGAILSLSPELFFSIDGSEIETRPIKGTLPR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 201 GVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFR 280
Cdd:TIGR00553 161 GADPQEDRAQASALAESAKDRAENLMIVDLLRNDLGRIAEVGSVKVPELFVVETYPTVHQLVSTITARLREDLTLSDLFR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 281 SLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGITWDSTWESEYRE 360
Cdd:TIGR00553 241 ALFPGGSITGAPKVRAMEIIDELEPQPRGVYCGAIGYLSPEGDMDFNVAIRTLTLDGGRAVYGVGGGIVADSDPEAEYRE 320


                  ....*...
gi 2039176577 361 VHQKAAVL 368
Cdd:TIGR00553 321 CLLKAAPL 328
PRK07508 PRK07508
aminodeoxychorismate synthase component I;
8-365 6.94e-133

aminodeoxychorismate synthase component I;


Pssm-ID: 236035 [Multi-domain]  Cd Length: 378  Bit Score: 392.45  E-value: 6.94e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577   8 DFRTLGERYTFTQPIKELKTRNVEEVADLLAQVESYQEQGYYVVGYVSYEAAPAFEEKLAvhkdPLLGEY----LLYFTV 83
Cdd:PRK07508    6 RDDPAGRAVLFADPSEIIRARTPDEFAPALAAMERARAAGKWLAGYLSYEAGYLLEPKLA----PLMPEGretpLLCFGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  84 HDS-VETSPIPLTYED-----IDLPSNWqevtSAADYEKAIAQIHHHLRQGDTYQVNYTVQLKQKLSANPFAIYNRMVVE 157
Cdd:PRK07508   82 FDApSPEAPAPARPSEnaarlRDPVARW----DFADYAQRFERLHRHIRAGDCYQANLTFPLDARWGGDPLALFWALAAR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 158 QEAGYNAYVEHDEMAVISMSPELFFE-QNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMN 236
Cdd:PRK07508  158 QPVGYGALVDLGGPVILSRSPELFFRvDGEGWIETHPMKGTAPRGATPAEDARLRAALLNDEKNQAENRMIVDLLRNDIS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 237 RISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIG 316
Cdd:PRK07508  238 RISEVGSLDVPELFDIETYPTVHQMVSRVRARLLPGLGLADIFAALFPCGSITGAPKIRAMEILRELEPGPRDLYCGAIG 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2039176577 317 LLLPNGRRIFNVAIRTIQLHK-GQAIYGVGGGITWDSTWESEYREVHQKA 365
Cdd:PRK07508  318 WIAPDGRMRFNVAIRTLSLFPgGRAVFNVGGGIVFDSTAEAEYEECLLKA 367
Chorismate_bind pfam00425
chorismate binding enzyme; This family includes the catalytic regions of the chorismate ...
 112-364 3.32e-113

chorismate binding enzyme; This family includes the catalytic regions of the chorismate binding enzymes anthranilate synthase, isochorismate synthase, aminodeoxychorismate synthase and para-aminobenzoate synthase.


Pssm-ID: 425674 [Multi-domain]  Cd Length: 255  Bit Score: 337.22  E-value: 3.32e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 112 ADYEKAIAQIHHHLRQGDTYQVNYTVQLKQKL--SANPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELFFEQNDREL 189
Cdd:pfam00425   1 EDYLAAVEKAKEAIRAGDLYKVVLSRRLTLPLagDIDPLALYRRLRARNPAPYSFYFRTGDFTFLGASPERLLSVDGGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 190 TTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQL 269
Cdd:pfam00425  81 ITEPIAGTRPRGKDPAEDEALAAELLADPKERAEHLMVVDLIRNDLGRVCVPGSVKVPELPEVERYGTVQHLVSTISGRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 270 REDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGIT 349
Cdd:pfam00425 161 KPGLSLLDLLKALFPTGAVTGAPKKRAMEIIRELEPFPRGLYAGAVGYLDPDGDADFAVAIRTALVDNGRARLYAGAGIV 240

                         250
                  ....*....|....*
gi 2039176577 350 WDSTWESEYREVHQK 364
Cdd:pfam00425 241 ADSDPEAEWEETEAK 255
TrpE COG0147
Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism, ...
 51-368 4.55e-109

Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthases component I is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439917 [Multi-domain]  Cd Length: 416  Bit Score: 332.84  E-value: 4.55e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  51 VGYVSYEAAPAFEEKLAVHKDPLlGEYLLYFTVHDSVetspipLTYediDLPSNWQEVTSAADYEKAIAQIHHHLRQGDT 130
Cdd:COG0147   103 VGYFGYDLVRYFERLPDLAPDDL-GLPDAALGLYDRL------LVF---DHLKGTRSNFTREEYLAAVERAKEYIRAGDI 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 131 YQVNYTVQLKQKLSANPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQ 210
Cdd:COG0147   173 FQVVLSQRFSAPFEGDPLALYRALRRINPSPYMFYLRFGDFAIVGSSPERLVRVEDGRVETRPIAGTRPRGATPEEDAAL 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 211 ASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITG 290
Cdd:COG0147   253 AEELLADEKERAEHLMLVDLARNDLGRVCEPGSVKVPELMVVERYSHVMHLVSTVTGRLRPGLDALDALRATFPAGTLTG 332

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2039176577 291 APKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGITWDSTWESEYREVHQKAAVL 368
Cdd:COG0147   333 APKIRAMEIIDELEPTRRGVYGGAVGYLSFDGNMDLAIAIRTAVVKDGRAYVQAGAGIVADSDPEAEYQETLNKARAL 410
PabB-clade2 TIGR01824
aminodeoxychorismate synthase, component I, clade 2; This clade of sequences is more closely ...
 35-368 1.79e-86

aminodeoxychorismate synthase, component I, clade 2; This clade of sequences is more closely related to TrpE (anthranilate synthase, TIGR00564/TIGR01820/TIGR00565) than to the better characterized group of PabB enzymes (TIGR00553/TIGR01823). This clade includes one characterized enzyme from Lactococcus and the conserved function across the clade is supported by these pieces of evidence: 1) all genomes with a member in this clade also have a separate TrpE gene, 2) none of these genomes contain an aparrent PabB from any of the other PabB clades, 3) none of these sequences are found in a region of the genome in association with other Trp biosynthesis genes, 4) all of these genomes aparrently contain most if not all of the steps of the folate biosynthetic pathway (for which PABA is a precursor). Many of the sequences hit by this model are annotated as TrpE enzymes, however, we believe that all members of this clade are, in fact, PabB. The sequences from Bacillus halodurans and subtilus which score below the trusted cutoff for this model are also likely to be PabB enzymes, but are too closely related to TrpE to be separated at this time.


Pssm-ID: 130883  Cd Length: 355  Bit Score: 272.42  E-value: 1.79e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  35 DLLAQVESY-----QEQGYYVVGYVSYEAAPAFEEK---LAVHKDPLLGEYLlYFTVHDSVET--SPIPLTYEDIDLPSN 104
Cdd:TIGR01824  10 DVARRLEGIpdlgtSDGGWPVAADFRYEAAVARDHQrqiVALATVPAETEGE-FATSSDQLPAvaAATSLPSPDVGPLPV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 105 WQEVTSA-ADYEKAIAQIHHHLRQGDTYQVNYTVQLKQKLSA--NPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELF 181
Cdd:TIGR01824  89 DLEASIDrAAYETGVRRIKDYIRAGDVFQANLSRRLTAPIAAdvDPLQLFLALRAPNPAPYAIYLEEPGVDVASASPELF 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 182 FEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQM 261
Cdd:TIGR01824 169 LAREGRVVQTRPIAGTRPRGATLAEDGALAAELLQHDKDRAEHVMIVDLERNDLGRVCATGTVRVPELCAVESYSHVHHL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 262 TSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAI 341
Cdd:TIGR01824 249 VSRVTGRLREGAGLADLIRALFPGGSITGAPKVRAMEIIDELEPQPRGPYTGSVGWIDADGNADLNILIRTLEGGGAQLH 328

                         330       340
                  ....*....|....*....|....*..
gi 2039176577 342 YGVGGGITWDSTWESEYREVHQKAAVL 368
Cdd:TIGR01824 329 FRTGAGIVADSDPAGEWDETEAKARAL 355
pabB PRK15465
aminodeoxychorismate synthase component 1;
78-364 7.11e-62

aminodeoxychorismate synthase component 1;


Pssm-ID: 185362 [Multi-domain]  Cd Length: 453  Bit Score: 210.93  E-value: 7.11e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  78 LLYFTVHDSVE--TSPIPLTYEDIDLPSNWQEVTSAADYEKAIAQIHHHLRQGDTYQVNYTVQLKQKLSANPFAIYNRMV 155
Cdd:PRK15465  155 LSHNDVNARRAwlESQQFSPQEDFTLTSDWQSNMTREQYGEKFRQVQEYLHSGDCYQVNLAQRFHATYSGDEWQAFLQLN 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 156 VEQEAGYNAYVEHDEMAVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDM 235
Cdd:PRK15465  235 QANRAPFSAFLRLEQGAILSLSPERFILCDNSEIQTRPIKGTLPRLPDPQEDSKQAEKLANSAKDRAENLMIVDLMRNDI 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 236 NRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTI 315
Cdd:PRK15465  315 GRVAVAGSVKVPELFVVEPFPAVHHLVSTITARLPEQLHASDLLRAAFPGGSITGAPKVRAMEIIDELEPQRRNAWCGSI 394

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2039176577 316 GLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGITWDSTWESEYREVHQK 364
Cdd:PRK15465  395 GYLSFCGNMDTSITIRTLTAINGQIYCSAGGGIVADSQEEAEYQETFDK 443
PRK05877 PRK05877
aminodeoxychorismate synthase component I; Provisional
 84-368 8.78e-58

aminodeoxychorismate synthase component I; Provisional


Pssm-ID: 235634 [Multi-domain]  Cd Length: 405  Bit Score: 198.77  E-value: 8.78e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  84 HDSVETSPIP------LTYEDIDLPSNWQEVTSAAD---YEKAIAQIHHHLRQGDTYQVNYTVQLKQKLSANPFAIYNRM 154
Cdd:PRK05877  105 YESLSGAPDPdwlasaLATTRARPAPPCRIDWTPPDraaHRDGVLACLEAIAAGEVYQACVCTQFTGTVTGSPLDFFADG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 155 VVEQEAGYNAYVEHDEMAVISMSPELFFEQNDRELTTRPMKGTTQRGvtdqedlEQASWLEQDPKNRSENMMIVDLLRND 234
Cdd:PRK05877  185 VARTAPARAAYLAGDWGAVASLSPELFLRRRGSVVTSSPIKGTLPLD-------ADPSALRASAKDVAENIMIVDLVRND 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 235 MNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGT 314
Cdd:PRK05877  258 LGRVARTGTVTVPELLVVRPAPGVWHLVSTVSAQVPDELPMSDLLDATFPPASVTGTPKLRARELISQWEPVRRGIYCGT 337

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2039176577 315 IGLLLPNGRRIFNVAIRTIQLHK-GQAIYGVGGGITWDSTWESEYREVHQKAAVL 368
Cdd:PRK05877  338 VGLASPVAGCELNVAIRTVEFDAdGNAVLGVGGGITADSDPDAEWQECLHKAAPI 392
PRK05940 PRK05940
anthranilate synthase component I;
90-365 9.21e-55

anthranilate synthase component I;


Pssm-ID: 235651 [Multi-domain]  Cd Length: 463  Bit Score: 192.25  E-value: 9.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  90 SPIPLTYEDIDLPSNWQEVtsaaDYEKAIAQIHHHLRQGDTYQVNYTVQLKQKLSANPFAIYNRMVVEQEAGYNAYVEHD 169
Cdd:PRK05940  172 LPLDLRTPPSSLIFYTTQQ----EYEAAVRQAKKYIQAGDIFQANLSLRFQTTTSADSWQIYRRLQQINPSPFASYWRTP 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 170 EMAVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERL 249
Cdd:PRK05940  248 WGDVVSCSPERLVQLQGNQAQTRPIAGTRPRGKTPAEDQQLAEELLSNIKERAEHIMLVDLERNDLGRVCQWGSVEVDEL 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 250 CQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVA 329
Cdd:PRK05940  328 LTIERYSHVIHLVSNVVGTLQPNRDAIDLIRALFPGGTITGCPKVRCMEIIEELEPVRRNLFYGSCGYLDQRGNLDLNIL 407

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2039176577 330 IRTI----QLHKGQAIYG-VGGGITWDSTWESEYREVHQKA 365
Cdd:PRK05940  408 IRTLlytpLSRGLSTIWGqVGAGIVADSDPEKEWLESLQKA 448
PLN02889 PLN02889
oxo-acid-lyase/anthranilate synthase
 109-376 2.85e-53

oxo-acid-lyase/anthranilate synthase


Pssm-ID: 215481 [Multi-domain]  Cd Length: 918  Bit Score: 195.07  E-value: 2.85e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 109 TSAADYEKAIAQIHHHLRQGDTYQVNYTVQLKQKL-SANPFAIYNRMVVEQEAGYNAYVE--HDEMAVISMSPELFFeQN 185
Cdd:PLN02889  641 KSREQYIKDVQKCLKYIKDGESYELCLTTQMRKRIgEIDSLGLYLHLREKNPAPYAAWLNfsNENLCICSSSPERFL-KL 719

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 186 DRE--LTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTS 263
Cdd:PLN02889  720 DRNgmLEAKPIKGTIARGSTPEEDEQLKLQLQYSEKDQAENLMIVDLLRNDLGRVCEPGSVHVPNLMDVESYTTVHTMVS 799

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 264 TIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYG 343
Cdd:PLN02889  800 TIRGKKRSNMSPVDCVRAAFPGGSMTGAPKLRSMELLDSLESSSRGIYSGSIGFFSYNQTFDLNIVIRTVVIHEGEASIG 879

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2039176577 344 VGGGITWDSTWESEYREVHQK------AAVLYRKQARFQ 376
Cdd:PLN02889  880 AGGAIVALSNPEDEYEEMILKtrapanAVIEFQKDQRSN 918
PRK09070 PRK09070
aminodeoxychorismate synthase component I;
114-370 4.83e-53

aminodeoxychorismate synthase component I;


Pssm-ID: 236371 [Multi-domain]  Cd Length: 447  Bit Score: 187.22  E-value: 4.83e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 114 YEKAIAQIHHHLRQGDTYQVNYTVQLKQKLSA--NPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELFFEQNDRELTT 191
Cdd:PRK09070  185 FTDGVERVLDYIRAGDVFQVNLSRAWQAQFANavDPAALYARLRAANPAPFSGLFVAAGRAIVSSSPERLVSVQGGVVQT 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 192 RPMKGTTQRGVtDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLRE 271
Cdd:PRK09070  265 RPIAGTRPRFA-GDDDAALIRELVGHPKERAEHVMLIDLERNDLGRICAPGSVEVDELMTVESYAHVHHIVSNVRGRLRD 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 272 DVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGITWD 351
Cdd:PRK09070  344 GVTPGEVIRAVFPGGTITGCPKVRCMQIIAELEQTPRGAYTGSFGYLNRDGDMDLNILIRTAEVQGNQVRFRTGAGIVVD 423

                         250
                  ....*....|....*....
gi 2039176577 352 STWESEYREVHQKAAVLYR 370
Cdd:PRK09070  424 SDPERELDETRAKARGLLR 442
PRK13571 PRK13571
anthranilate synthase component I; Provisional
 109-368 8.38e-49

anthranilate synthase component I; Provisional


Pssm-ID: 184152 [Multi-domain]  Cd Length: 506  Bit Score: 176.75  E-value: 8.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 109 TSAADYEKAIAQIHHHLRQGDTYQVNYTVQLKQKLSANPFAIYnRMV-------------VEQEAGYNAYvehdemAVIS 175
Cdd:PRK13571  227 RTVEEFGAAVEKLVEEIRAGEAFQVVPSQRFEMDTTADPLDVY-RVLrvtnpspymyllrVPNSDGGTDF------SIVG 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 176 MSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQY 255
Cdd:PRK13571  300 SSPEALVTVTDGRATTHPIAGTRWRGATPEEDALLEKELLADPKERAEHLMLVDLGRNDLGRVCRPGTVRVVDFSHIERY 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 256 STVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQL 335
Cdd:PRK13571  380 SHVMHLVSTVTGELAEGRTALDAVTACFPAGTLSGAPKVRAMELIEELEPTRRGLYGGVVGYLDFAGDADTAIAIRTALM 459

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2039176577 336 HKGQAIYGVGGGITWDSTWESEYREVHQKA-AVL 368
Cdd:PRK13571  460 RDGTAYVQAGGGVVADSDPDYEDNEARNKAaAVL 493
PRK13574 PRK13574
anthranilate synthase component I; Provisional
 50-368 4.40e-46

anthranilate synthase component I; Provisional


Pssm-ID: 184155 [Multi-domain]  Cd Length: 420  Bit Score: 167.30  E-value: 4.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  50 VVGYVSYEAAPAFE----EKLAVHKDPllgeYLLYFT-----VHDSVETSpiplTYEDIDLP-------------SNWQE 107
Cdd:PRK13574   82 MIGYISYDAVRFWEkirdLKPAAEDWP----YAEFFIpdniiIYDHNEGK----VYVNGDLSsvggcgdmgefkiSFYDE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 108 VTSAADYEKAIAQIHHHLRQGDTYQVNYTVQLKQKLSANPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELFFEQNDR 187
Cdd:PRK13574  154 SLNKNNYEKIVSESLEYIRSGYIFQVVLSRFYRYLFSGDPLRIYYNLRRINPSPYMFYLKFDERYLIGSSPELLFRVQDN 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 188 ELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKS 267
Cdd:PRK13574  234 IVETYPIAGTRPRGSDQEEDLKLELELMNSEKDKAEHLMLVDLARNDLGKVCVPGTVRVPELMYVEKYSHVQHIVSKVIG 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 268 QLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGG 347
Cdd:PRK13574  314 TLKKKYNALDVLKATFPAGTVSGAPKPMAMNIIETLEEYKRGPYAGAVGFISADGNAEFAIAIRTAFLNKDLLRIQAGAG 393

                         330       340
                  ....*....|....*....|.
gi 2039176577 348 ITWDSTWESEYREVHQKAAVL 368
Cdd:PRK13574  394 IVYDSNPESEYFETEHKLRAL 414
PLN02445 PLN02445
anthranilate synthase component I
 113-370 1.12e-45

anthranilate synthase component I


Pssm-ID: 215244 [Multi-domain]  Cd Length: 523  Bit Score: 168.70  E-value: 1.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 113 DYEKAIAQIHHHLRQGDTYQVNYTVQLKQKLSANPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELFFEQNDRELTTR 192
Cdd:PLN02445  237 EYKNAVLQAKEHILAGDIFQIVLSQRFERRTFADPFEVYRALRIVNPSPYMIYLQARGCILVASSPEILTRVKKNKIVNR 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 193 PMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLRED 272
Cdd:PLN02445  317 PLAGTRRRGKTPEEDKALEKDLLADEKQCAEHIMLVDLGRNDVGKVSKAGSVKVEKLMNIERYSHVMHISSTVTGELLDH 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 273 VDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQL---HKGQAIYG------ 343
Cdd:PLN02445  397 LTSWDALRAALPVGTVSGAPKVRAMELIDELEVTRRGPYSGGFGGVSFTGDMDIALALRTMVFptaARYDTMYSykdtns 476

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2039176577 344 ---------VGGGITWDSTWESEYREVHQKAAVLYR 370
Cdd:PLN02445  477 rrewvahlqAGAGIVADSDPEDEYRECVNKAAGLAR 512
PRK13572 PRK13572
anthranilate synthase component I; Provisional
 3-368 2.73e-44

anthranilate synthase component I; Provisional


Pssm-ID: 237432 [Multi-domain]  Cd Length: 435  Bit Score: 162.98  E-value: 2.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577   3 RKTVIDfrtlGERYT-FTQPIKELKTRNVEEVADllaqveSYQEQGYyvVGYVSYEAAPAFEEKlAVHKDPLLGEYLLYF 81
Cdd:PRK13572   54 NKTKVD----GETISkESNPFKALKENFKITQSG------DRFTGGF--VGYIAYDAVHNYIGG-KIEEPSVFGYYDHVF 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  82 tVHD---------SVETSPIPLTY----------EDIDLPSNWQEVTSA----ADYEKAIAQIHHHLRQGDTYQVNYTVQ 138
Cdd:PRK13572  121 -VYDhvtrkfyfhSLNNNPEELFNaekivekakrFEIEEEDGGSEVLGCdadrEEFVEMVEKAKEYIYSGDVFQVVLSRE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 139 LKQKLSANPFAIYNRMVVEQEAGYNAYVEHDEmAVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDP 218
Cdd:PRK13572  200 YRLKTDLSPFQLYRNLREINPSPYMFLLEFDK-DVVGASPETMASVENNILKINPIAGTAPRGKTEEEDKKLAEALLSDE 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 219 KNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATME 298
Cdd:PRK13572  279 KERAEHVMLVDLARNDVRKVSKSGSVRLERFFDVVKYSHVQHIESEVVGELKEDSTMFDAIEAAFPAGTLTGAPKFRAME 358

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2039176577 299 IIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYgVGGGITWDSTWESEYREVHQK-AAVL 368
Cdd:PRK13572  359 IIDELEKSRRKVYGGAVGYFSNSGNADLAIAIRMAEIDKVCRVR-AGAGIVADSVPEKEFYETERKmAAVL 428
PRK07093 PRK07093
para-aminobenzoate synthase component I; Validated
 81-364 5.11e-44

para-aminobenzoate synthase component I; Validated


Pssm-ID: 235932 [Multi-domain]  Cd Length: 323  Bit Score: 159.26  E-value: 5.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  81 FTVHDSVETSPIPLTYEDIDLPsnwqevtsAADYEKAIAQIHHHLRQGDTYQVNYTVQLKQKLSANPFAIYNRmvveQEA 160
Cdd:PRK07093   51 KTNVPSQVRPHKPFELQKEPIS--------FEEYQQGFELVQEEIQAGNSYLLNLTYPTPIETNLSLEEIFQA----SKA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 161 GYNAYVEHDemaVISMSPELFFEQNDRELTTRPMKGTTQrgvtdqEDLEQAS-WLEQDPKNRSENMMIVDLLRNDMNRIS 239
Cdd:PRK07093  119 KYKLLFKDQ---FVCFSPEPFVRIEDNKISTYPMKGTID------ASLPNAEeKLLNDEKEFAEHATIVDLLRNDLSMVA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 240 E-VgseHVERLCQVEQYST----VWQMTSTIKSQLREDVD--LVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYC 312
Cdd:PRK07093  190 KnV---RVTRFRYIDKIKTnkgeILQTSSEISGTLPENWQenIGDILAKLLPAGSITGAPKEKTVEIIEQAEGYERGFYT 266

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2039176577 313 GTIGlllpngrrIFN-------VAIRTIQLHKGQAIYGVGGGITWDSTWESEYREVHQK 364
Cdd:PRK07093  267 GVFG--------YFDgesldsaVMIRFIEQENDGLYFKSGGGITIDSDLKDEYNELIQK 317
PRK13567 PRK13567
anthranilate synthase component I; Provisional
 92-368 1.85e-43

anthranilate synthase component I; Provisional


Pssm-ID: 184148 [Multi-domain]  Cd Length: 468  Bit Score: 161.47  E-value: 1.85e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  92 IPLTYEDIDLPSNWQEVTSAADYEKAIA---QIHHHLRQGDTYQV------NYTVQLKQKLSANPFAIYNRMVVEQEAGY 162
Cdd:PRK13567  178 IQPFMPTQDFDFKTKEIQSNISEERFIEmiqYFKEKITEGDMFQVvpsriyKYAHHASQHLNQLSFQLYQNLKRQNPSPY 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 163 NAYVEHDEMAVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVG 242
Cdd:PRK13567  258 MYYLNIDQPYIVGSSPESFVSVKDQIVTTNPIAGTIQRGETTQIDNENMKQLLNDPKECSEHRMLVDLGRNDIHRVSKIG 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 243 SEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNG 322
Cdd:PRK13567  338 TSKITKLMVIEKYEHVMHIVSEVTGKINQNLSPMTVIANLLPTGTVSGAPKLRAIERIYEQYPHKRGVYSGGVGYINCNH 417

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2039176577 323 RRIFNVAIRTIQLHKGQAIYGVGGGITWDSTWESEYREVHQKAAVL 368
Cdd:PRK13567  418 NLDFALAIRTMMIDEQYINVEAGCGVVYDSIPEKELNETKLKAKSL 463
PRK06404 PRK06404
anthranilate synthase component I; Reviewed
 54-365 2.25e-34

anthranilate synthase component I; Reviewed


Pssm-ID: 102361 [Multi-domain]  Cd Length: 351  Bit Score: 133.46  E-value: 2.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  54 VSYEAAPA-FEEKLAVHKDPllgeYLLYFtVHDSVETSPIPLT-YEDIDLPSNWQEVtsaaDYEKAIAQIHHHLRQGDTY 131
Cdd:PRK06404   54 VTYDFVNAcFNNKVEKSGWP----YFYSM-DPETSYKRNIERKsFKTVKLKGNYNDI----SLSLKIKELIELIRAGEVL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 132 QVNYTVQLKQKLsaNPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQA 211
Cdd:PRK06404  125 QVVISREFEANI--DFKEKLSEFINNDRSRYVFYYRFGKYRVVGSSPENVFTVNGNIINVDPIAGTYDDKILSNELLNSE 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 212 swleqdpKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLrEDVDLVEIFRSLFPCGSITGA 291
Cdd:PRK06404  203 -------KDKLEHRMLLDLARNDLSKFADIGTLNVDKVMKIEEFSSVKHLVSQVTAKF-SNASYRDILASMFPAGTVSGS 274

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2039176577 292 PKIATMEIIKNLEPQPRGVYCGTIGLLlpnGRRIFNVA--IRTIQLHKGQAIYGVGGGITWDSTWESEYREVHQKA 365
Cdd:PRK06404  275 PKERAIEIINKYEETPRGPYGGAIGII---SKGYTDMAlvIRTAYSHGNGFRVRAGAGIVKDSDPEDEVNEIYSKA 347
PRK07546 PRK07546
hypothetical protein; Provisional
 375-570 7.14e-33

hypothetical protein; Provisional


Pssm-ID: 169002 [Multi-domain]  Cd Length: 209  Bit Score: 125.09  E-value: 7.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 375 FQLITTgeisqknLLFE--------DQHLERLRKASRYFAFPFDAEDLGHKIEEECQDCEANQdyRLRISLSKSGEIEVN 446
Cdd:PRK07546    4 FELIET-------LRWEpgagfprlDRHLARLERSARALGFPCDPAAVRAKLAEAVAGAQGPL--RLRLTLARDGRLTVE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 447 RQVLTPLSTSfCQAQVCLQEAALNQS--FTYFKTTHRP--------HLSLGEQEKIYHNKSGELLETSIGNLVLKIAGKL 516
Cdd:PRK07546   75 TAPLPPLPPD-TVWRVAIARTRLDSAdpLLRYKTTRRAaydaaraeLPPAEADEVILLNERGEVCEGTITNVFLDRGGGM 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2039176577 517 Y-TPPIRLGILPGIYRQHLLETGQVEEKVLTLADLTQAEAIYGCNAVRGLYELSL 570
Cdd:PRK07546  154 LtTPPLSCGLLPGVLRAELLDAGRAREAVLTVDDLKSARAIWVGNSLRGLIRAEL 208
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 376-566 2.36e-31

Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 121.31  E-value: 2.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 376 QLITTGEISQKNLLFEDQHLERLRKASRYFA--FPFDAEDLGHKIEEeCQDCEANQDYRLRISLSKSGE------IEVNR 447
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGipLPFDEEDLRKIIEE-LLKANGLGVGRLRLTVSRGPGgfglptSDPTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 448 QV----LTPLSTSFCQA-QVCLQEAALNQSFTYFKTTHRP--------HLSLGEQEKIYHNKSGELLETSIGNLVLKIAG 514
Cdd:pfam01063  80 AIfvsaLPPPPESKKKGvISSLVRRNPPSPLPGAKTLNYLenvlarreAKAQGADDALLLDEDGNVTEGSTSNVFLVKGG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2039176577 515 KLYTPPIRLGILPGIYRQHLLETGQ-----VEEKVLTLADLTQAEAIYGCNAVRGLY 566
Cdd:pfam01063 160 TLYTPPLESGILPGITRQALLDLAKalgleVEERPITLADLQEADEAFLTNSLRGVT 216
PRK13564 PRK13564
anthranilate synthase component 1;
110-368 2.23e-30

anthranilate synthase component 1;


Pssm-ID: 237428 [Multi-domain]  Cd Length: 520  Bit Score: 124.95  E-value: 2.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 110 SAADYEKAIAQIHHHLRQGDTYQVnytVqLKQKLSA---NPFAIYNRMVVEQEAGYNAYVEHDEMAVISMSPE--LFFEQ 184
Cdd:PRK13564  241 SDEEFCAVVRKLKEHIRAGDIFQV---V-PSRRFSLpcpSPLAAYRVLKKSNPSPYMFYMQDEDFTLFGASPEsaLKYDA 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 185 NDRELTTRPMKGTTQRGVTDQE--DLEQASWLE----QDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTV 258
Cdd:PRK13564  317 SSRQVEIYPIAGTRPRGRRADGsiDRDLDSRIElelrTDHKELAEHLMLVDLARNDLARICQPGSRYVADLLKVDRYSHV 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 259 WQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKG 338
Cdd:PRK13564  397 MHLVSRVVGELRHDLDALHAYRACMNMGTLTGAPKVRAMQLIREVEGQRRGSYGGAVGYLTGHGDLDTCIVIRSAFVENG 476

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2039176577 339 QAIYGVGGGITWDSTWESEYREVHQKA-AVL 368
Cdd:PRK13564  477 IATVQAGAGVVLDSDPQSEADETRNKAqAVL 507
PRK13566 PRK13566
anthranilate synthase component I;
147-370 2.92e-21

anthranilate synthase component I;


Pssm-ID: 237429 [Multi-domain]  Cd Length: 720  Bit Score: 98.07  E-value: 2.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 147 PFAIYNRMVVEQEAGYNAYVE-HDEMAVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENM 225
Cdd:PRK13566  279 PSEIFRRLKEINPSPYGFFINlGDGEYLVGASPEMFVRVEGRRVETCPISGTIKRGADAIGDAEQIRKLLNSKKDESELT 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 226 MIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEP 305
Cdd:PRK13566  359 MCTDVDRNDKSRVCEPGSVKVIGRRQIEMYSRLIHTVDHVEGRLRPGFDALDAFLTHAWAVTVTGAPKLWAMQFIEDHER 438

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2039176577 306 QPRGVYCGTIGLLLPNGRriFN--VAIRTIQLHKGQAIYGVGGGITWDSTWESEYREVHQKAAVLYR 370
Cdd:PRK13566  439 SPRRWYGGAVGMVGFDGD--MNtgLTLRTIRIKDGVAEVRVGATLLFDSDPEAEEAETELKASALLQ 503
PRK07054 PRK07054
isochorismate synthase;
177-360 4.15e-17

isochorismate synthase;


Pssm-ID: 235920 [Multi-domain]  Cd Length: 475  Bit Score: 84.05  E-value: 4.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 177 SPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEV----GSEHVERLCQV 252
Cdd:PRK07054  262 TPERLVRVAAGDLHTHALAGTIARGADPAEDARLGAALMASAKDRLEHALVVDAIRAALAPLSRAldipDQPSLHRLPRL 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 253 EQYSTvwqmtsTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRT 332
Cdd:PRK07054  342 QHLST------PIRATLAPDATLLQVVAALHPTPAVGGHPRAAALDYIRAHEGFDRGWYAAPIGWLDAHGNGDFAVALRS 415

                         170       180
                  ....*....|....*....|....*...
gi 2039176577 333 IQLHKGQAIYGVGGGITWDSTWESEYRE 360
Cdd:PRK07054  416 ALITGGACRLFAGCGIVADSEPASEYRE 443
PRK06772 PRK06772
salicylate synthase;
114-366 1.45e-16

salicylate synthase;


Pssm-ID: 102546 [Multi-domain]  Cd Length: 434  Bit Score: 82.09  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 114 YEKAIAQIHHHLRQGDTYQV--NYTVQLKQKLSANPFAIYNRMVVEQEAGYNAYVEHDEmaVISMSPELFFEQNDRELTT 191
Cdd:PRK06772  175 YKQQVARAVAEIRRGEYVKVivSRAIPLPSRIDMPATLLYGRQANTPVRSFMFRQEGRE--ALGFSPELVMSVTGNKVVT 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 192 RPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQYSTVWQMTSTIKSQLRE 271
Cdd:PRK06772  253 EPLAGTRDRMGNPEHNKAKEAELLHDSKEVLEHILSVKEAIAELEAVCQPGSVVVEDLMSVRQRGSVQHLGSGVSGQLAE 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 272 DVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIgLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGITWD 351
Cdd:PRK06772  333 NKDAWDAFTVLFPSITASGIPKNAALNAIMQIEKTPRELYSGAI-LLLDDTRFDAALVLRSVFQDSQRCWIQAGAGIIAQ 411

                         250
                  ....*....|....*
gi 2039176577 352 STWESEYREVHQKAA 366
Cdd:PRK06772  412 STPERELTETREKLA 426
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 377-565 4.25e-16

ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.


Pssm-ID: 238800 [Multi-domain]  Cd Length: 249  Bit Score: 78.12  E-value: 4.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 377 LITTGEISQKNLLFEDQHLERLRKASRYFAFPFDAEDlghKIEEECQDCEANQDY---RLRISLS-----KSGEIEVNR- 447
Cdd:cd01559    10 VFETMRALDGRLFLLDAHLARLERSARRLGIPEPDLP---RLRAALESLLAANDIdegRIRLILSrgpggRGYAPSVCPg 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 448 ----QVLTPLSTSFCQAQV----CLQEAALNQSFTYFKTTHR--PHLSL------GEQEKIYHNKSGELLETSIGNLVLK 511
Cdd:cd01559    87 palyVSVIPLPPAWRQDGVrlitCPVRLGEQPLLAGLKHLNYleNVLAKreardrGADEALFLDTDGRVIEGTASNLFFV 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2039176577 512 IAGKLYTPPIRLGILPGIYRQHLLETG-----QVEEKVLTLADLTQAEAIYGCNAVRGL 565
Cdd:cd01559   167 KDGELVTPSLDRGGLAGITRQRVIELAaakgyAVDERPLRLEDLLAADEAFLTNSLLGV 225
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 388-565 4.31e-16

Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439885 [Multi-domain]  Cd Length: 285  Bit Score: 78.69  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 388 LLFEDQHLERLRKASR--YFAFPFDAEDLghkiEEECQD-CEAN--QDYRLRISLS--------KSGEIEVNRQVLT-PL 453
Cdd:COG0115    41 LFRLDEHLARLNRSAKrlGIPIPYTEEEL----LEAIRElVAANglEDGYIRPQVTrgvggrgvFAEEYEPTVIIIAsPL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 454 STSFCQAQ-------VCLQEAALNQSFTYFKTTHRPHLSLGEQEK--------IYHNKSGELLETSIGNLVLKIAGKLYT 518
Cdd:COG0115   117 PAYPAEAYekgvrviTSPYRRAAPGGLGGIKTGNYLNNVLAKQEAkeagadeaLLLDTDGYVAEGSGSNVFIVKDGVLVT 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2039176577 519 PPIRLGILPGIYRQHLLE----TG-QVEEKVLTLADLTQAEAIYGCNAVRGL 565
Cdd:COG0115   197 PPLSGGILPGITRDSVIElareLGiPVEERPISLEELYTADEVFLTGTAAEV 248
PRK07912 PRK07912
salicylate synthase;
177-368 3.29e-15

salicylate synthase;


Pssm-ID: 169151 [Multi-domain]  Cd Length: 449  Bit Score: 77.91  E-value: 3.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 177 SPELFFE-QNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVDLLRNDMNRISEVGSEHVERLCQVEQY 255
Cdd:PRK07912  249 SPELVTAvRADGVVITEPLAGTRAFGRGAAIDRLARDDLESNSKEIVEHAISVRSSLAEITEIAEPGSAAVIDFMTVRER 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 256 STVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQL 335
Cdd:PRK07912  329 GSVQHLGSTVRGRLDASSDRMDALEALFPAVTASGIPKAAGVDAIFRLDEAPRGLYSGAVVMLSADGGLDAALTLRAAYQ 408

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2039176577 336 HKGQAIYGVGGGITWDSTWESEYREVHQKAAVL 368
Cdd:PRK07912  409 VGGRTWLRAGAGIIEESEPEREFEETCEKLSTL 441
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 387-565 3.70e-13

PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.


Pssm-ID: 238254 [Multi-domain]  Cd Length: 256  Bit Score: 69.55  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 387 NLLFEDQHLERLRKASRYFAFP--FDAEDLgHKIEEECQDCEANQDYRLRISLSKSGEiEVNRQVLTPLSTSFCQA--QV 462
Cdd:cd00449    20 RLFRLDEHLDRLNRSAKRLGLPipYDREEL-REALKELVAANNGASLYIRPLLTRGVG-GLGVAPPPSPEPTFVVFasPV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 463 CLQEAALNQSF-TYFKTTHRPH-----------------------LSLGEQEKIYHNKSGELLETSIGNLVLKIAGKLYT 518
Cdd:cd00449    98 GAYAKGGEKGVrLITSPDRRRAapggtgdaktggnlnsvlakqeaAEAGADEALLLDDNGYVTEGSASNVFIVKDGELVT 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2039176577 519 PPIRLGILPGIYRQHLLETGQ-----VEEKVLTLADLTQAEAIYGCNAVRGL 565
Cdd:cd00449   178 PPLDGGILPGITRDSVIELAKelgikVEERPISLDELYAADEVFLTGTAAEV 229
PRK15016 PRK15016
isochorismate synthase EntC; Provisional
 149-360 1.19e-12

isochorismate synthase EntC; Provisional


Pssm-ID: 184977 [Multi-domain]  Cd Length: 391  Bit Score: 69.90  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 149 AIYNRMVVEQEAGYNAYVE-HDEMAVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMI 227
Cdd:PRK15016  166 ALLERLIAQNPVSYNFHVPlADGGVLLGASPELLLRKDGERFSSLPLAGSARRQPDEVLDREAGNRLLASEKDRHEHELV 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 228 V----DLLRNDMNRISEVGSEhverlcQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNL 303
Cdd:PRK15016  246 TqamkEVLRERSSELHVPSSP------QLITTPTLWHLATPFEGKANAQENALTLACLLHPTPALSGFPHQAAKQVIAEL 319

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2039176577 304 EPQPRGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGITWDSTWESEYRE 360
Cdd:PRK15016  320 EPFDRELFGGIVGWCDSEGNGEWVVTIRCAKLRENQVRLFAGAGIVPASSPLGEWRE 376
PRK06923 PRK06923
isochorismate synthase DhbC; Validated
 84-364 5.27e-12

isochorismate synthase DhbC; Validated


Pssm-ID: 235886 [Multi-domain]  Cd Length: 399  Bit Score: 67.84  E-value: 5.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577  84 HDSVETSPIPLTYEdidlpsnWQEVTSAADYEKAIAQIHHHLRQGD--------TYQVNYTVQL-KQKLSANpFAIYNRm 154
Cdd:PRK06923  101 TTNHLEINRNLTFE-------MTPVPDPEVYMNGVKQGIAKIQDGDlkkivlsrSLDVKSSEKIdKQKLLRE-LAEHNK- 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 155 vveqeAGYNAYV----EHDEM--AVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIV 228
Cdd:PRK06923  172 -----HGYTFAVnlpkDENENskTLIGASPELLVSRHGMQVISNPLAGSRPRSDDPVEDKRRAEELLSSPKDLHEHAVVV 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 229 DLLRNDMNRISEVgsEHVERLCQVEQYSTVWQMTSTIKSQLRE-DVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQP 307
Cdd:PRK06923  247 EAVAAALRPYCHT--LHVPEKPSVIHTEAMWHLSTEVKGELKDpNTSSLELAIALHPTPAVCGTPTEEAREAIQQIEPFD 324

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2039176577 308 RGVYCGTIGLLLPNGRRIFNVAIRTIQLHKGQAIYGVGGGITWDSTWESEYREVHQK 364
Cdd:PRK06923  325 REFFTGMLGWSDLNGDGEWIVTIRCAEVEENTLRLYAGAGVVAESKPEDELAETSAK 381
PLN02786 PLN02786
isochorismate synthase
 146-366 3.70e-11

isochorismate synthase


Pssm-ID: 178383 [Multi-domain]  Cd Length: 533  Bit Score: 65.58  E-value: 3.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 146 NPFAIYNRMVVEQEAGYNAYVE-HDEMAVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSEN 224
Cdd:PLN02786  298 DPIAWLACLQVEGQNAYQFCLQpPDAPAFIGNTPEQLFHRKGLGVCSEALAATRPRGGSSARDLQIELDLLTSPKDDLEF 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 225 MMIVDLLRNDMNRI-SEVgseHVERLCQVEQYSTVWQMTSTIKSQLREDVDLVEIFRSLFPCGSITGAPKIATMEIIKNL 303
Cdd:PLN02786  378 SIVRENIREKLEAIcDRV---VVEPHKAIRKLARVQHLYAQLAGRLRSEDDEFDILAALHPTPAVCGHPTEEARLLIAET 454

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2039176577 304 EPQPRGVYCGTIGlLLPNGRRIFNVAIRTIQLHKGQA--IYGvGGGITWDSTWESEYREVHQKAA 366
Cdd:PLN02786  455 ESFDRGMYAGPVG-WFGGGESEFAVGIRSALVEKGLGalIYA-GTGIVEGSNPSSEWNELELKIS 517
PRK15012 PRK15012
menaquinone-specific isochorismate synthase; Provisional
 172-368 2.91e-10

menaquinone-specific isochorismate synthase; Provisional


Pssm-ID: 184974 [Multi-domain]  Cd Length: 431  Bit Score: 62.55  E-value: 2.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 172 AVISMSPELFFEQNDRELTTRPMKGTTQRGVTDQEDLEQASWLEQDPKNRSENMMIVD----LLRNDMNRIsEVGSEHVE 247
Cdd:PRK15012  233 AFLGSSPERLWRRRDKALRTEALAGTVANHPDDKQAQQLGEWLMADDKNQRENMLVVEdicqRLQADTQTL-DVLPPQVL 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 248 RLCQVEqystvwQMTSTIKSQLREdVDLVEIFRSLFPCGSITGAPKIATMEIIKNLEPQPRGVYCGTIGLLLPNGRRiFN 327
Cdd:PRK15012  312 RLRKVQ------HLRRCIWTSLNK-ADDVICLHQLQPTAAVAGLPRDLARQFIARHEPFTREWYAGSAGYLSLQQSE-FC 383

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2039176577 328 VAIRTIQLHKGQAIYGVGGGITWDSTWESEYREVHQKAAVL 368
Cdd:PRK15012  384 VSLRSAKVSGNVVRLYAGAGIVRGSDPEQEWQEIDNKAAGL 424
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 487-556 1.08e-07

D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes transamination between D-amino acids and their respective alpha-keto acids. It plays a major role in the synthesis of bacterial cell wall components like D-alanine and D-glutamate in addition to other D-amino acids. The enzyme like other members of this superfamily requires PLP as a cofactor. Members of this subgroup are found in all three forms of life.


Pssm-ID: 238799 [Multi-domain]  Cd Length: 270  Bit Score: 53.37  E-value: 1.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2039176577 487 GEQEKIYHNKSGELLETSIGNLVLKIAGKLYTPPIRLGILPGIYRQHLLETGQ-----VEEKVLTLADLTQA-EAI 556
Cdd:cd01558   160 GADEAILLDADGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKelgipVEERPFSLEELYTAdEVF 235
PRK07101 PRK07101
hypothetical protein; Provisional
 496-565 4.27e-06

hypothetical protein; Provisional


Pssm-ID: 235934  Cd Length: 187  Bit Score: 47.63  E-value: 4.27e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 496 KSGELLETSIGNLVLKIAGKLYTPPIRLgiLPGIYRQHLLETGQVEEKVLTLADLTQAEAIYGCNAVRGL 565
Cdd:PRK07101  120 KNGLVTDTSIGNLAFFDGKQWFTPKKPL--LKGTQRARLLDEGKIKEKDITVEDLLQYEEIRLINAMNGF 187
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
 487-556 5.15e-06

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 48.33  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 487 GEQEKIYHNKSGELLETSIGNLVLKIAGKLYTPPIRLGILPGIYRQHLLETGQ-----VEEKVLTLADL----------T 551
Cdd:PRK08320  169 GVDEAIMLNDEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKelgipVREELFTLHDLytadevfltgT 248


                  ....*
gi 2039176577 552 QAEAI 556
Cdd:PRK08320  249 AAEVI 253
PRK06092 PRK06092
4-amino-4-deoxychorismate lyase; Reviewed
 497-565 1.10e-05

4-amino-4-deoxychorismate lyase; Reviewed


Pssm-ID: 235696  Cd Length: 268  Bit Score: 47.14  E-value: 1.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2039176577 497 SGELLETSIGNLVLKIAGKLYTPPIRLGILPGIYRQHLLETGQ-----VEEKVLTLADLTQAEAIYGCNAVRGL 565
Cdd:PRK06092  168 EGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAqsgypVVEVDASLEELLQADEVFICNSLMPV 241
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
 480-565 4.15e-05

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 45.73  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 480 HRPHLslgeqEKIYHNKSGELLETSIGNLVLKIAGKLYTPPIRLGILPGIYRQHLLETGQ-----VEEKVLTLADLTQAE 554
Cdd:PRK07650  160 NDPNK-----EGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEelgieVKEGFYTKEELLSAD 234

                          90
                  ....*....|.
gi 2039176577 555 AIYGCNAVRGL 565
Cdd:PRK07650  235 EVFVTNSIQEI 245
PRK07849 PRK07849
aminodeoxychorismate lyase;
492-564 1.24e-04

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 44.18  E-value: 1.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2039176577 492 IYHNKSGELLETSIGNLVLKIAGKLYTPPIRLGILPGIYRQHLLETG-----QVEEKVLTLADLTQAEAIYGCNAVRG 564
Cdd:PRK07849  182 IFTSTDGYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVArekgwDCEYRALRPADLFAADGVWLVSSVRL 259
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
 495-559 2.04e-04

BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life.


Pssm-ID: 238798  Cd Length: 279  Bit Score: 43.34  E-value: 2.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039176577 495 NKSGELLETSIGNLVLKIAGKLYTPPIRLGILPGIYRQHLLETGQ-----VEEKVLTLADLTQAEAIYGC 559
Cdd:cd01557   169 GAHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARdlgikVEERPITRDELYEADEVFAT 238
 
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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