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Conserved domains on  [gi|1361143906|ref|WP_106341359|]
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aspartate carbamoyltransferase catalytic subunit [Laceyella sediminis]

Protein Classification

aspartate carbamoyltransferase( domain architecture ID 11425422)

aspartate carbamoyltransferase catalyzes the conversion of aspartate and carbamoyl phosphate to carbamoyl-L-aspartate, the first unique step of pyrimidine biosynthesis

CATH:  3.40.50.1370
EC:  2.1.3.2
Gene Ontology:  GO:0004070|GO:0006520|GO:0016597|GO:0016743
SCOP:  4000794

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 8-308 6.79e-160

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


:

Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 447.96  E-value: 6.79e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906   8 WKREHLLDTSQLTLNELKAILARARYWEENWRPG--MGPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSS 85
Cdd:COG0540     3 FKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIkkVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTSS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  86 TAKGESLYDTVKTLASLGVEVAVIRHSDPEQVKALARqEVGCKILNAGAGHWAHPTQALLDLYTMLKHFVDLSGKTVAIV 165
Cdd:COG0540    83 VSKGESLADTIRTLEAYGADAIVIRHPQEGAARLLAE-HVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAIV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 166 GDIAHSRVVHSNMWSLKRFGAHVILSGPQAMRDRDCEQE--APYVPFEEALQTADVVMMLRVQLERHQEKLFTSKQDYHK 243
Cdd:COG0540   162 GDLKHSRVARSNIKALSKLGAEVTLVAPPTLLPEEIEELgvEVTTDLDEALPDADVVYMLRIQKERFTDGLFPSYREYKR 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1361143906 244 QYGLTLQRLRLMKPEAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLEHALEGEK 308
Cdd:COG0540   242 SYGLTAERLALAKPDAIVMHPGPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGGEE 306
 
Name Accession Description Interval E-value
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 8-308 6.79e-160

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 447.96  E-value: 6.79e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906   8 WKREHLLDTSQLTLNELKAILARARYWEENWRPG--MGPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSS 85
Cdd:COG0540     3 FKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIkkVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTSS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  86 TAKGESLYDTVKTLASLGVEVAVIRHSDPEQVKALARqEVGCKILNAGAGHWAHPTQALLDLYTMLKHFVDLSGKTVAIV 165
Cdd:COG0540    83 VSKGESLADTIRTLEAYGADAIVIRHPQEGAARLLAE-HVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAIV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 166 GDIAHSRVVHSNMWSLKRFGAHVILSGPQAMRDRDCEQE--APYVPFEEALQTADVVMMLRVQLERHQEKLFTSKQDYHK 243
Cdd:COG0540   162 GDLKHSRVARSNIKALSKLGAEVTLVAPPTLLPEEIEELgvEVTTDLDEALPDADVVYMLRIQKERFTDGLFPSYREYKR 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1361143906 244 QYGLTLQRLRLMKPEAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLEHALEGEK 308
Cdd:COG0540   242 SYGLTAERLALAKPDAIVMHPGPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGGEE 306
pyrB PRK00856
aspartate carbamoyltransferase catalytic subunit;
8-308 2.50e-157

aspartate carbamoyltransferase catalytic subunit;


Pssm-ID: 234849 [Multi-domain]  Cd Length: 305  Bit Score: 441.43  E-value: 2.50e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906   8 WKREHLLDTSQLTLNELKAILARARYWEENWRPGMGPY---RGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVS 84
Cdd:PRK00856    3 LKMKHLLSIEDLSREEIELLLDTAEEFKEVLRREVKKVpllRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  85 STAKGESLYDTVKTLASLGVEVAVIRHSDpEQVKALARQEVGCKILNAGAGHWAHPTQALLDLYTMLKHFVDLSGKTVAI 164
Cdd:PRK00856   83 SVSKGETLADTIRTLSAMGADAIVIRHPQ-SGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 165 VGDIAHSRVVHSNMWSLKRFGAHVILSGPQAMRDRDCEQEAPYVPFEEALQTADVVMMLRVQLERHQEKLFTSKQDYHKQ 244
Cdd:PRK00856  162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTLLPEGMPEYGVHTDLDEVIEDADVVMMLRVQKERMDGGLLPSYEEYKRS 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1361143906 245 YGLTLQRLRLMKPEAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLEHALEGEK 308
Cdd:PRK00856  242 YGLTAERLALAKPDAIVMHPGPVNRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGGRL 305
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 11-305 2.13e-106

aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273209 [Multi-domain]  Cd Length: 301  Bit Score: 311.99  E-value: 2.13e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  11 EHLLDTSQLTLNELKAILARARYWEENWRPGMGPYR--GRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPD-VSSTA 87
Cdd:TIGR00670   1 RHLISISDLSREEIELLLETARELEQVLNGKEPLKLlkGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSDSeTSSVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  88 KGESLYDTVKTLASLgVEVAVIRHSDpEQVKALARQEVGCKILNAGAGHWAHPTQALLDLYTMLKHFVDLSGKTVAIVGD 167
Cdd:TIGR00670  81 KGETLADTIKTLSGY-VDAIVIRHPL-EGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 168 IAHSRVVHSNMWSLKRFGAHVILSGPQAMRDRDCEQEA---------PYVPFEEALQTADVVMMLRVQLERHQekLFTSK 238
Cdd:TIGR00670 159 LKYGRTVHSLAEALTRFGVEVYLISPEELRMPKEILEElkakgikvrETESLEEVIDEADVLYVTRIQKERFP--DPEEY 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1361143906 239 QDYHKQYGLTLQRLRLMKPEAIIMHPGPfnRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLEHALE 305
Cdd:TIGR00670 237 EKVKGSYGITLERLEAAKKGVIIMHPLP--RVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
OTCace_N pfam02729
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
12-151 1.15e-47

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;


Pssm-ID: 460665 [Multi-domain]  Cd Length: 140  Bit Score: 156.43  E-value: 1.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  12 HLLDTSQLTLNELKAILARARYWEENWRPGMG--PYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSSTAKG 89
Cdd:pfam02729   1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKlpLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1361143906  90 ESLYDTVKTLASLgVEVAVIRHSDPEQVKALARqEVGCKILNAGAGHWaHPTQALLDLYTML 151
Cdd:pfam02729  81 ESLADTARVLSRY-VDAIVIRHFGHEDLEELAE-YASVPVINAGGDHE-HPTQALADLLTIR 139
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 155-261 9.51e-06

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240639 [Multi-domain]  Cd Length: 307  Bit Score: 46.29  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 155 VDLSGKTVAIVG---------DIAHSrvvhsnmwslkrFGAHVILSGPQAMRDRDceqeAPYVPFEEALQTADVVmMLRV 225
Cdd:cd12162   143 IELAGKTLGIIGygnigqavaRIARA------------FGMKVLFAERKGAPPLR----EGYVSLDELLAQSDVI-SLHC 205

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1361143906 226 QLERHQEKLFTSKqdyhkqygltlqRLRLMKPEAII 261
Cdd:cd12162   206 PLTPETRNLINAE------------ELAKMKPGAIL 229
 
Name Accession Description Interval E-value
PyrB COG0540
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ...
 8-308 6.79e-160

Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440306 [Multi-domain]  Cd Length: 306  Bit Score: 447.96  E-value: 6.79e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906   8 WKREHLLDTSQLTLNELKAILARARYWEENWRPG--MGPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSS 85
Cdd:COG0540     3 FKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIkkVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTSS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  86 TAKGESLYDTVKTLASLGVEVAVIRHSDPEQVKALARqEVGCKILNAGAGHWAHPTQALLDLYTMLKHFVDLSGKTVAIV 165
Cdd:COG0540    83 VSKGESLADTIRTLEAYGADAIVIRHPQEGAARLLAE-HVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAIV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 166 GDIAHSRVVHSNMWSLKRFGAHVILSGPQAMRDRDCEQE--APYVPFEEALQTADVVMMLRVQLERHQEKLFTSKQDYHK 243
Cdd:COG0540   162 GDLKHSRVARSNIKALSKLGAEVTLVAPPTLLPEEIEELgvEVTTDLDEALPDADVVYMLRIQKERFTDGLFPSYREYKR 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1361143906 244 QYGLTLQRLRLMKPEAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLEHALEGEK 308
Cdd:COG0540   242 SYGLTAERLALAKPDAIVMHPGPRNRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGGEE 306
pyrB PRK00856
aspartate carbamoyltransferase catalytic subunit;
8-308 2.50e-157

aspartate carbamoyltransferase catalytic subunit;


Pssm-ID: 234849 [Multi-domain]  Cd Length: 305  Bit Score: 441.43  E-value: 2.50e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906   8 WKREHLLDTSQLTLNELKAILARARYWEENWRPGMGPY---RGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVS 84
Cdd:PRK00856    3 LKMKHLLSIEDLSREEIELLLDTAEEFKEVLRREVKKVpllRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSASTS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  85 STAKGESLYDTVKTLASLGVEVAVIRHSDpEQVKALARQEVGCKILNAGAGHWAHPTQALLDLYTMLKHFVDLSGKTVAI 164
Cdd:PRK00856   83 SVSKGETLADTIRTLSAMGADAIVIRHPQ-SGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 165 VGDIAHSRVVHSNMWSLKRFGAHVILSGPQAMRDRDCEQEAPYVPFEEALQTADVVMMLRVQLERHQEKLFTSKQDYHKQ 244
Cdd:PRK00856  162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTLLPEGMPEYGVHTDLDEVIEDADVVMMLRVQKERMDGGLLPSYEEYKRS 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1361143906 245 YGLTLQRLRLMKPEAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLEHALEGEK 308
Cdd:PRK00856  242 YGLTAERLALAKPDAIVMHPGPVNRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGGRL 305
asp_carb_tr TIGR00670
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ...
 11-305 2.13e-106

aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273209 [Multi-domain]  Cd Length: 301  Bit Score: 311.99  E-value: 2.13e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  11 EHLLDTSQLTLNELKAILARARYWEENWRPGMGPYR--GRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPD-VSSTA 87
Cdd:TIGR00670   1 RHLISISDLSREEIELLLETARELEQVLNGKEPLKLlkGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSDSeTSSVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  88 KGESLYDTVKTLASLgVEVAVIRHSDpEQVKALARQEVGCKILNAGAGHWAHPTQALLDLYTMLKHFVDLSGKTVAIVGD 167
Cdd:TIGR00670  81 KGETLADTIKTLSGY-VDAIVIRHPL-EGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 168 IAHSRVVHSNMWSLKRFGAHVILSGPQAMRDRDCEQEA---------PYVPFEEALQTADVVMMLRVQLERHQekLFTSK 238
Cdd:TIGR00670 159 LKYGRTVHSLAEALTRFGVEVYLISPEELRMPKEILEElkakgikvrETESLEEVIDEADVLYVTRIQKERFP--DPEEY 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1361143906 239 QDYHKQYGLTLQRLRLMKPEAIIMHPGPfnRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLEHALE 305
Cdd:TIGR00670 237 EKVKGSYGITLERLEAAKKGVIIMHPLP--RVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
pyrB PRK13814
aspartate carbamoyltransferase;
12-301 4.43e-64

aspartate carbamoyltransferase;


Pssm-ID: 139876 [Multi-domain]  Cd Length: 310  Bit Score: 204.57  E-value: 4.43e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  12 HLLDTSQLTLNELKAILARARYW-----EENwrPGMGPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSST 86
Cdd:PRK13814    7 HLLNMRSLTRDHIEKLIQRANYFltqgmEKN--SVFETLKGHVVANLFFEPSTRTRNSFEIAAKRLGAMVLNPNLKISAI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  87 AKGESLYDTVKTLASLGVEVAVIRHSDPEQVKALARQEVGCKILNAGAGHWAHPTQALLDLYTMLKHFVDLSGKTVAIVG 166
Cdd:PRK13814   85 SKGETLFDTIKTLEAMGVYFFIVRHSENETPEQIAKQLSSGVVINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 167 DIAHSRVVHSNMWSLKRFGA-HVILSGPQAMRDRDCEQEA--PYVPFEEALQTADVVMMLRVQLERHQEKLftSKQDYHK 243
Cdd:PRK13814  165 DIRHSRVANSLMDGLVTMGVpEIRLVGPSSLLPDKVGNDSikKFTELKPSLLNSDVIVTLRLQKERHDNSV--DIDAFRG 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1361143906 244 QYGLTLQRLRLMKPEAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLE 301
Cdd:PRK13814  243 SFRLTPEKLYSAKPDAIVMHPGPVNREVEINSDVADNQQSVILQQVRNGVAMRMAVLE 300
PLN02527 PLN02527
aspartate carbamoyltransferase
 11-306 9.77e-51

aspartate carbamoyltransferase


Pssm-ID: 178142 [Multi-domain]  Cd Length: 306  Bit Score: 169.93  E-value: 9.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  11 EHLLDTSQLTLNELKAILARARYWEENWR--PGMGPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNF--TPDVSST 86
Cdd:PLN02527    1 SDVIEAQQFDREMLELLFEVAREMEKVERgsPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLTTenAGEFSSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  87 AKGESLYDTVKTLASLgVEVAVIRHSDPEQVKALArqEVGCK-ILNAGAGHWAHPTQALLDLYTMLKHFVDLSGKTVAIV 165
Cdd:PLN02527   81 AKGETLEDTIRTVEGY-SDIIVLRHFESGAARRAA--ATAEIpVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 166 GDIAHSRVVHSNMWSLKRF-GAHVILSGPQAMRDRDCEQE---APYVPFEE------ALQTADVVMMLRVQLERHQEKLf 235
Cdd:PLN02527  158 GDLANGRTVRSLAYLLAKYeDVKIYFVAPDVVKMKDDIKDyltSKGVEWEEssdlmeVASKCDVLYQTRIQRERFGERI- 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1361143906 236 tskQDYHK---QYGLTLQRLRLMKPEAIIMHPGPfnRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLEHALEG 306
Cdd:PLN02527  237 ---DLYEAargKYIVDKKVMDVLPKHAVVMHPLP--RLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLLGG 305
OTCace_N pfam02729
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
12-151 1.15e-47

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;


Pssm-ID: 460665 [Multi-domain]  Cd Length: 140  Bit Score: 156.43  E-value: 1.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  12 HLLDTSQLTLNELKAILARARYWEENWRPGMG--PYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSSTAKG 89
Cdd:pfam02729   1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKlpLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1361143906  90 ESLYDTVKTLASLgVEVAVIRHSDPEQVKALARqEVGCKILNAGAGHWaHPTQALLDLYTML 151
Cdd:pfam02729  81 ESLADTARVLSRY-VDAIVIRHFGHEDLEELAE-YASVPVINAGGDHE-HPTQALADLLTIR 139
ArgF COG0078
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine ...
 12-306 7.34e-47

Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine carbamoyltransferase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439848 [Multi-domain]  Cd Length: 310  Bit Score: 159.83  E-value: 7.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  12 HLLDTSQLTLNELKAILARARYWEENWRPGM--GPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSSTAKG 89
Cdd:COG0078     7 HFLSLLDLTPEELRALLDLAAELKAKRKAGIphRPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIYLDPGDSQLGRG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  90 ESLYDTVKTLASLgVEVAVIRHSDPEQVKALARqevgckilnagaghWA------------HPTQALLDLYTMLKHFVDL 157
Cdd:COG0078    87 ESIKDTARVLSRY-VDGIMIRTFGHETLEELAK--------------YAgvpvingltdlfHPCQALADLLTIREHFGKL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 158 SGKTVAIVGDiaHSRVVHSNMWSLKRFGAHVILSGP------QAMRDRdCEQEA------------PyvpfEEALQTADV 219
Cdd:COG0078   152 KGLKVAYVGD--GNNVANSLLLAAAKLGMDVRIATPegyepdPEIVAK-AKEIAaesggsitithdP----AEAVKGADV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 220 V-------MmlrvqlerHQEKLFTSKQDYHKQYGLTLQRLRLMKPEAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANG 292
Cdd:COG0078   225 VytdvwvsM--------GQEEEAEERIKAFKPYQVNEELMALAKPDAIFMHCLPAHRGEEVTDEVIDGPQSVVFDEAENR 296

                         330
                  ....*....|....
gi 1361143906 293 VWIRMAVLEHALEG 306
Cdd:COG0078   297 LHAQKALLAWLLGG 310
PRK08192 PRK08192
aspartate carbamoyltransferase; Provisional
 11-298 1.83e-44

aspartate carbamoyltransferase; Provisional


Pssm-ID: 169269 [Multi-domain]  Cd Length: 338  Bit Score: 154.50  E-value: 1.83e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  11 EHLLDTSQLTLNELKAILARARyweenwrpGMGPY----------RGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFT 80
Cdd:PRK08192    6 SHILSVNQLDRDAIQRIFNVAD--------RMEPYalrekrtrvlEGAILGNLFFEPSTRTRVSFGCAFNLLGGHVRETT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  81 P-DVSSTAKGESLYDTVKTLASLGvEVAVIRHSDPEQVKALARqevGCKI--LNAGAGHWAHPTQALLDLYTM---LKHF 154
Cdd:PRK08192   78 GmASSSLSKGESLYDTARVLSTYS-DVIAMRHPDAGSVKEFAE---GSRVpvINGGDGSNEHPTQALLDLFTIqkeLAHA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 155 -VDLSGKTVAIVGDIAHSRVVHSNMWSLKRF-GAHVILSGPQ--AMRDR---DCEQEAPYVPFEEALQT----ADVVMML 223
Cdd:PRK08192  154 gRGIDGMHIAMVGDLKFGRTVHSLSRLLCMYkNVSFTLVSPKelAMPDYvisDIENAGHKITITDQLEGnldkADILYLT 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 224 RVQLERhqeklFTSKQDYHKQYGltlqRLRL--------MKPEAIIMHPGPFN---RGVEVADEVVEHPRSKIFEQKANG 292
Cdd:PRK08192  234 RIQEER-----FPSQEEANKYRG----KFRLnqsiytqhCKSNTVIMHPLPRDsraQANELDNDLNSHPNLAIFRQADNG 304


                  ....*.
gi 1361143906 293 VWIRMA 298
Cdd:PRK08192  305 LLIRMA 310
orni_carb_tr TIGR00658
ornithine carbamoyltransferase; This family of ornithine carbamoyltransferases (OTCase) is in ...
 12-301 1.71e-42

ornithine carbamoyltransferase; This family of ornithine carbamoyltransferases (OTCase) is in a superfamily with the related enzyme aspartate carbamoyltransferase. Most known examples are anabolic, playing a role in arginine biosynthesis, but some are catabolic. Most OTCases are homotrimers, but the homotrimers are organized into dodecamers built from four trimers in at least two species; the catabolic OTCase of Pseudomonas aeruginosa is allosterically regulated, while OTCase of the extreme thermophile Pyrococcus furiosus shows both allostery and thermophily. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 129743 [Multi-domain]  Cd Length: 304  Bit Score: 148.27  E-value: 1.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  12 HLLDTSQLTLNELKAILARARYWEENWRPGM--GPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSSTAKG 89
Cdd:TIGR00658   2 HLLSLLDLSPEEIRYLLQLAKKLKKGKKKGKehKKLKGKTLALIFEKPSTRTRVSFEVAAYQLGGHPLYLNPNDLQLGRG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  90 ESLYDTVKTLASL--GVEVAVIRHSDpeqVKALARqEVGCKILNaGAGHWAHPTQALLDLYTMLKHFVDLSGKTVAIVGD 167
Cdd:TIGR00658  82 ESIKDTARVLSRYvdGIMARVYKHED---VEELAK-YASVPVIN-GLTDLFHPCQALADLLTIIEHFGKLKGVKVVYVGD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 168 iaHSRVVHSNMWSLKRFGAHVILSGPQAmrdrdCEQEAPYVPF------------------EEALQTADVVMMlRVQLER 229
Cdd:TIGR00658 157 --GNNVCNSLMLAGAKLGMDVVVATPEG-----YEPDADIVKKaqeiakenggsvelthdpVEAVKGADVIYT-DVWVSM 228

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1361143906 230 HQEKLFTSKQDYHKQYGLTLQRLRLMKPEAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLE 301
Cdd:TIGR00658 229 GEEDKKEERLKLFRPYQVNEELMELAKPEVIFMHCLPAHRGEEVTDEVIEGPHSIVFDQAENRLHAQKAVMV 300
PRK11891 PRK11891
aspartate carbamoyltransferase; Provisional
 47-299 2.78e-41

aspartate carbamoyltransferase; Provisional


Pssm-ID: 183362 [Multi-domain]  Cd Length: 429  Bit Score: 148.09  E-value: 2.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  47 GRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTP-DVSSTAKGESLYDTVKTLASLgVEVAVIRHSDPEQVKALARqEV 125
Cdd:PRK11891  126 GAVLGNLFFEASTRTRVSFGAAFCRLGGSVCDTTGfTFSSMAKGESIYDTSRVMSGY-VDALVIRHPEQGSVAEFAR-AT 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 126 GCKILNAGAGHWAHPTQALLDLYTMLKHFVDLsGKTV-----AIVGDIAHSRVVHS--NMWSLKRFGAHVILSGPQ---- 194
Cdd:PRK11891  204 NLPVINGGDGPGEHPSQALLDLYTIQREFSRL-GKIVdgahiALVGDLKYGRTVHSlvKLLALYRGLKFTLVSPPTlemp 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 195 -------AMRDRDCEQEApyvPFEEALQTADVVMMLRVQLERHQEKLFtskQDYHKQYGLTLQRL-RLMKPEAIIMHPGP 266
Cdd:PRK11891  283 ayiveqiSRNGHVIEQTD---DLAAGLRGADVVYATRIQKERFADESF---EGYTPDFQINQALVdAVCKPDTLIMHPLP 356

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1361143906 267 FNR---GVEVADEVVEHPRSKIFEQKANGVWIRMAV 299
Cdd:PRK11891  357 RDSrpgANDLSTDLNRDPRLAIFRQTDNGIPVRMAI 392
PRK00779 PRK00779
ornithine carbamoyltransferase; Provisional
 12-304 8.14e-35

ornithine carbamoyltransferase; Provisional


Pssm-ID: 234835 [Multi-domain]  Cd Length: 304  Bit Score: 127.90  E-value: 8.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  12 HLLDTSQLTLNELKAILARARYWEENWRPGMG--PYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSSTAKG 89
Cdd:PRK00779    6 HFLSLDDLSPEELEELLDLAAELKKKRKAGEPhpPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIFLSPRDTQLGRG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  90 ESLYDTVKTLASLgVEVAVIR---HSDPEQVKALARQEVgckiLNAGAGHwAHPTQALLDLYTMLKHFVDLSGKTVAIVG 166
Cdd:PRK00779   86 EPIEDTARVLSRY-VDAIMIRtfeHETLEELAEYSTVPV----INGLTDL-SHPCQILADLLTIYEHRGSLKGLKVAWVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 167 D---IAHSRVVHSNMwslkrFGAHVILSGP------QAMRDRDCEQEAPYVPF----EEALQTADVV-------M-MLRV 225
Cdd:PRK00779  160 DgnnVANSLLLAAAL-----LGFDLRVATPkgyepdPEIVEKIAKETGASIEVthdpKEAVKGADVVytdvwvsMgQEAE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 226 QLERHqeKLFtskqdyhKQYGLTLQRLRLMKPEAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANgvwiRM----AVLE 301
Cdd:PRK00779  235 AEERL--KAF-------APYQVNEELMALAKPDAIFMHCLPAHRGEEVTDEVIDGPQSVVWDEAEN----RLhaqkALLA 301


                  ...
gi 1361143906 302 HAL 304
Cdd:PRK00779  302 WLL 304
OTCace pfam00185
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
161-302 1.14e-31

Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;


Pssm-ID: 425511 [Multi-domain]  Cd Length: 154  Bit Score: 115.40  E-value: 1.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 161 TVAIVGDiAHSRVVHSNMWSLKRFGAHVILSGPQAMRDR---------DCEQEAPYVPF----EEALQTADVVMMLRVQL 227
Cdd:pfam00185   1 KIAYVGD-GHNNVAHSLIIAAAKLGMDVRLATPKGYPPDpevldkakkIAEKSGGSIEItddpAEAVKGADVVYTDVWQS 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1361143906 228 ERHQEKLFTSKQDYhKQYGLTLQRLRLMKPEAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLEH 302
Cdd:pfam00185  80 MGQEKEREERLKAF-KPYQVNEELMKLAKKDAIFMHCLPAHRGEEVTDDVFDGPRSVVFDQAENRLHAQKALLAL 153
PLN02342 PLN02342
ornithine carbamoyltransferase
 9-304 3.32e-28

ornithine carbamoyltransferase


Pssm-ID: 177976 [Multi-domain]  Cd Length: 348  Bit Score: 111.42  E-value: 3.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906   9 KREHLLDTSQLTLNELKAILARARYWEENWRPG---MGPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSS 85
Cdd:PLN02342   44 KPKHFLHIDDFDKEEILGLLDRAKEVKALLKSGdrsFQPFKGKSMAMIFTKPSMRTRVSFETGFFLLGGHALYLGPDDIQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  86 TAKGESLYDTVKTLASLG--VEVAVIRHSDPEQVKALARQEVgckiLNaGAGHWAHPTQALLDLYTMLKHFVDLSGKTVA 163
Cdd:PLN02342  124 LGKREETRDIARVLSRYNdiIMARVFAHQDVLDLAEYSSVPV----IN-GLTDYNHPCQIMADALTIIEHIGRLEGTKVV 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 164 IVGDiaHSRVVHSNMWSLKRFGAHVILSGPQAmrdrdceqeapYVPFEEALQTADVVMMLRVQLE-------RHQEKLFT 236
Cdd:PLN02342  199 YVGD--GNNIVHSWLLLAAVLPFHFVCACPKG-----------YEPDAKTVEKARAAGISKIEITndpaeavKGADVVYT 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 237 -------SKQDYHKQY----GLTLQRlRLMK---PEAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLEH 302
Cdd:PLN02342  266 dvwasmgQKEEAEKRKkafqGFQVNE-ALMKlagPQAYFMHCLPAERGVEVTDGVMEAPNSIVFPQAENRMHAQNAIMLH 344


                  ..
gi 1361143906 303 AL 304
Cdd:PLN02342  345 QL 346
PRK02102 PRK02102
ornithine carbamoyltransferase; Validated
 11-304 1.82e-22

ornithine carbamoyltransferase; Validated


Pssm-ID: 179366 [Multi-domain]  Cd Length: 331  Bit Score: 95.34  E-value: 1.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  11 EHLLDTSQltlnELKAiLARARYWEEnwrpgmgPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSSTAKGE 90
Cdd:PRK02102   22 EYLIDLSI----ELKA-AKKAGIEHQ-------YLEGKNIALIFEKTSTRTRCAFEVAAIDLGAHVTYLGPNDSQLGKKE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  91 SLYDTVKTLASL--GVEvavIRHSDPEQVKALARQEvGCKILNAGAGHWaHPTQALLDLYTMLKHFVDLSGKTVAIVGDi 168
Cdd:PRK02102   90 SIEDTARVLGRMydGIE---YRGFKQEIVEELAKYS-GVPVWNGLTDEW-HPTQMLADFMTMKEHFGPLKGLKLAYVGD- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 169 AHSRVVHSNMWSLKRFGAHVILSGPQAMRDRD-----CEQEA------------PyvpfEEALQTADV------VMMlrv 225
Cdd:PRK02102  164 GRNNMANSLMVGGAKLGMDVRICAPKELWPEEelvalAREIAketgakititedP----EEAVKGADViytdvwVSM--- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 226 qlerHQEKLFTSKQDYHKQYGLTLQRLRLM-KPEAIIMH--PGPFN---------------RGVEVADEVVEHPRSKIFE 287
Cdd:PRK02102  237 ----GEEDEWEERIKLLKPYQVNMDLMKATgNPDVIFMHclPAFHDtetkvgkeiaekyglKGLEVTDEVFESKYSIVFD 312

                         330       340
                  ....*....|....*....|.
gi 1361143906 288 QKANgvwiRM----AVLEHAL 304
Cdd:PRK02102  313 EAEN----RMhtikAVMVATL 329
PRK14805 PRK14805
ornithine carbamoyltransferase; Provisional
 11-304 2.17e-19

ornithine carbamoyltransferase; Provisional


Pssm-ID: 237819 [Multi-domain]  Cd Length: 302  Bit Score: 86.28  E-value: 2.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  11 EHLLDTSQLTLNELKAILARARYWEENwrPGmgPYR----GRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSST 86
Cdd:PRK14805    2 KHLLSIKELTQQQLLDLLALAKTIKAN--PA--EYRqalaGKSVVMLFEKPSLRTRVSFDIGINKLGGHCLYLDQQNGAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  87 AKGESLYDTVKTLASL--GVEVAVIRHSDPEQVKALARQEVgckiLNAGAGHWaHPTQALLDLYTMLKHFVDLSGKTVAI 164
Cdd:PRK14805   78 GKRESVADFAANLSCWadAIVARVFSHSTIEQLAEHGSVPV----INALCDLY-HPCQALADFLTLAEQFGDVSKVKLAY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 165 VGDiaHSRVVHSNMWSLKRFGAHVILSGPQAmrdrdceqeapYVPfeealqTADVVMMLRVQLERHQEKLFTSK-----Q 239
Cdd:PRK14805  153 VGD--GNNVTHSLMYGAAILGATMTVICPPG-----------HFP------DGQIVAEAQELAAKSGGKLVLTSdieaiE 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 240 DYHKQYGLT---------LQRLR-----------LMKPEAI--IMHPGPFNRGVEVADEVVEHPRSKIFEQKANGVWIRM 297
Cdd:PRK14805  214 GHDAIYTDTwismgddtpLAEIKakfapyqvnkaLMEKAGAtfVMHCQPAHRGVEITSEVMDGEGSLILQQAENRMHAQN 293


                  ....*..
gi 1361143906 298 AVLEHAL 304
Cdd:PRK14805  294 AVLVTLL 300
pyrB PRK13376
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase ...
 53-300 3.21e-19

bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase regulatory subunit; Provisional


Pssm-ID: 237369 [Multi-domain]  Cd Length: 525  Bit Score: 87.89  E-value: 3.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  53 LFFEPSTRTRFSFEVAEK-KLGMEVVNFTPDVSSTAKGESLYDTVKTLASLGVEVAVIRHSDPEQVKALARQEVGC---- 127
Cdd:PRK13376   56 VFVEPSTRTKESFINAAKfHKNVKVNIFDSEHSSFNKQESYTDTFNMLTGYSDYSIFIVRTRLEGVCRLLEEKVSEfasr 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 128 ------KILNAGAGHWAHPTQALLDLYTMLKHF-VDLSGKTVAIVGDIAHSRVVHSNMWSLKRFG-AHVILSGPQA---- 195
Cdd:PRK13376  136 ngievpAFINAGDGKHEHPTQELLDEFTFLEQNnFDNSFIHIALVGDLLHGRTVHSKVNGLKIFKnVKVDLIAPEElamp 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 196 ------MRDRDCEQEApYVPFEEALQTADVVMM---LRVQLERHQEKLFTSKQDYHKQYGLTLQRLRLMKPEAIIMHPGP 266
Cdd:PRK13376  216 ehyvekMKKNGFEVRI-FSSIEEYLSQKDVAKIwyfTRLQLERMGEDILEKEHILRKAVTFRKEFLDKLPEGVKFYHPLP 294

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1361143906 267 FNRgvevadevvEHPRSKIF----------EQKANGVWIRMAVL 300
Cdd:PRK13376  295 RHK---------VYPTIPTFldtlplngweTQAINGYWVRIVLL 329
PRK14804 PRK14804
ornithine carbamoyltransferase; Provisional
 11-305 2.05e-15

ornithine carbamoyltransferase; Provisional


Pssm-ID: 173265 [Multi-domain]  Cd Length: 311  Bit Score: 75.45  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  11 EHLLDTSQLTLNELKAILARARYWEENWRPGMGPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNftpdVSSTAKGE 90
Cdd:PRK14804    7 KHLISWEDWSDSEILDLLDFAVHVKKNRVNYAGHMSGRSLAMLFQKTSTRTRVSFEVAMTEMGGHGIY----LDWMASNF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  91 SLYDTVKTLASLGVEVAVI-----RHSDpeqvKALARQEVGCKILNaGAGHWAHPTQALLDLYT--MLKHFVDLSGKTVA 163
Cdd:PRK14804   83 QLSDIDLEARYLSRNVSVImarlkKHED----LLVMKNGSQVPVIN-GCDNMFHPCQSLADIMTiaLDSPEIPLNQKQLT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 164 IVGdiAHSRVVHSNMWSLKRFGAHVILSGPQAMRDR------DCEQEAPYVPFEE----ALQTADVVMM-LRVQLERHQE 232
Cdd:PRK14804  158 YIG--VHNNVVNSLIGITAALGIHLTLVTPIAAKENihaqtvERAKKKGTLSWEMnlhkAVSHADYVYTdTWLDMEFFND 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 233 KLFTSKQDyhkqygltlQRLRLMKP-----------EAIIMHPGPFNRGVEVADEVVEHPRSKIFEQKANGVWIRMAVLE 301
Cdd:PRK14804  236 PSYADKKK---------QRMELMMPyqinsslmektNAKVMHDMPIHAGYEITREVVLSDRSIIFQQAENRLDAQKAVIL 306


                  ....
gi 1361143906 302 HALE 305
Cdd:PRK14804  307 KLLE 310
PRK01713 PRK01713
ornithine carbamoyltransferase; Provisional
 4-304 4.82e-15

ornithine carbamoyltransferase; Provisional


Pssm-ID: 167263 [Multi-domain]  Cd Length: 334  Bit Score: 74.25  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906   4 MTQEWKREHLLDTSQLTLNELKAILARARYWEENWRPGMGPYR--GRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTP 81
Cdd:PRK01713    1 MAFNLKNRHLLSLVNHTEREIKYLLDLSRDLKRAKYAGTEQQRlkGKNIALIFEKTSTRTRCAFEVAAYDQGAQVTYIDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  82 DVSSTAKGESLYDTVKTLASL--GVEVaviRHSDPEQVKALARQEvGCKILNaGAGHWAHPTQALLDLYTMLKHFVD-LS 158
Cdd:PRK01713   81 NSSQIGHKESMKDTARVLGRMydAIEY---RGFKQSIVNELAEYA-GVPVFN-GLTDEFHPTQMLADVLTMIENCDKpLS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 159 GKTVAIVGDiAHSRVVHSNMWSLKRFGAHVILSGPQAMRDRD-----CEQEA----PYVPFEEALQTA---------DVV 220
Cdd:PRK01713  156 EISYVYIGD-ARNNMGNSLLLIGAKLGMDVRICAPKALLPEAslvemCEKFAkesgARITVTDDIDKAvkgvdfvhtDVW 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 221 MMLRVQLERHQEKLftskqDYHKQYGLTLQRL-RLMKPEAIIMHPGP-------------------FNRGVEVADEVVEH 280
Cdd:PRK01713  235 VSMGEPLETWGERI-----KLLMPYQVTPELMkRTGNPKVKFMHCLPafhnsetkvgrqiaekypeLANGIEVTEDVFES 309

                         330       340
                  ....*....|....*....|....
gi 1361143906 281 PRSKIFEQKANGVWIRMAVLEHAL 304
Cdd:PRK01713  310 PMNIAFEQAENRMHTIKAVMVASL 333
PRK04523 PRK04523
N-acetylornithine carbamoyltransferase; Reviewed
 12-301 2.50e-14

N-acetylornithine carbamoyltransferase; Reviewed


Pssm-ID: 235304 [Multi-domain]  Cd Length: 335  Bit Score: 72.47  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  12 HLLDTSQLTLNELKAILARARYWEENwrPGMGPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPD--------- 82
Cdd:PRK04523    5 HFLNTQDWSRAELDALLTQAAAFKRN--KLGSALKGKSIALVFFNPSLRTRTSFELGAFQLGGHAVVLQPGkdawpiefe 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  83 ---VSSTAKGESLYDTVKTLASLgVEVAVIRHSDPEQVKALARQEVgckILNAGAGH----------WAHPTQALLDLYT 149
Cdd:PRK04523   83 lgaVMDGETEEHIREVARVLSRY-VDLIGVRAFPKFVDWSKDRQDQ---VLNSFAKYstvpvinmetITHPCQELAHALA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 150 MLKHFVD-LSGKTVAIVGdIAHSR-----VVHSNMWSLKRFGAHVILSGPQ----------AMRDRDCEQEAPYVPF--- 210
Cdd:PRK04523  159 LQEHFGTtLRGKKYVLTW-TYHPKplntaVANSALLIATRLGMDVTLLCPTpdyilderymDWAEQNAAESGGSLTVshd 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 211 -EEALQTADVVMM-----LRVQLERHQEKLFTSKqdyHKQYGLTLQRLRLMKpEAIIMHPGPFNRGVEVADEVVEHPRSK 284
Cdd:PRK04523  238 iDSAYAGADVVYAkswgaLPFFGNWEPEKPIRDQ---YQHFIVDERKMALTN-NGVFSHCLPLRRNVKVTDAVMDSPNCI 313

                         330
                  ....*....|....*..
gi 1361143906 285 IFEQKANGVWIRMAVLE 301
Cdd:PRK04523  314 AIDEAENRLHVQKAIMA 330
PRK12562 PRK12562
ornithine carbamoyltransferase subunit F; Provisional
 7-300 7.48e-13

ornithine carbamoyltransferase subunit F; Provisional


Pssm-ID: 105755  Cd Length: 334  Bit Score: 68.16  E-value: 7.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906   7 EWKREHLLDTSQLTLNELKAILARARYWEENWRPGMGPYR--GRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVS 84
Cdd:PRK12562    3 GFYKKHFLKLLDFTPAELNSLLQLAAKLKADKKNGKEVARltGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  85 STAKGESLYDTVKTLASL--GVEVaviRHSDPEQVKALArQEVGCKILNaGAGHWAHPTQALLDLYTMLKHfvdLSGK-- 160
Cdd:PRK12562   83 QIGHKESIKDTARVLGRMydGIQY---RGHGQEVVETLA-EYAGVPVWN-GLTNEFHPTQLLADLLTMQEH---LPGKaf 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 161 ---TVAIVGDiAHSRVVHSNMWSLKRFGAHVILSGPQAmrdrdCEQEAPYVPFEEALQ---------TADVVMMLR---- 224
Cdd:PRK12562  155 nemTLVYAGD-ARNNMGNSMLEAAALTGLDLRLVAPQA-----CWPEASLVAECSALAqkhggkitlTEDIAAGVKgadf 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 225 ------VQLERHQEKlFTSKQDYHKQYGLTLQRLRLM-KPEAIIMHPGP------------------FNRGVEVADEVVE 279
Cdd:PRK12562  229 iytdvwVSMGEPKEK-WAERIALLRGYQVNSKMMALTgNPQVKFLHCLPafhddqttlgkkmakefgLHGGMEVTDEVFE 307

                         330       340
                  ....*....|....*....|.
gi 1361143906 280 HPRSKIFEQKANGVWIRMAVL 300
Cdd:PRK12562  308 SPASIVFDQAENRMHTIKAVM 328
PRK03515 PRK03515
ornithine carbamoyltransferase subunit I; Provisional
 4-178 2.28e-12

ornithine carbamoyltransferase subunit I; Provisional


Pssm-ID: 179587 [Multi-domain]  Cd Length: 336  Bit Score: 66.66  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906   4 MTQEWKReHLLDTSQLTLNELKAILARARYWEENWRPG--MGPYRGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTP 81
Cdd:PRK03515    1 MNQFYQR-HFLRLLDFTPAELNSLLQLAAKLKADKKNGkeEQKLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  82 DVSSTAKGESLYDTVKTLASL--GVEVaviRHSDPEQVKALArQEVGCKILNaGAGHWAHPTQALLDLYTMLKHFVD--L 157
Cdd:PRK03515   80 SGSQIGHKESIKDTARVLGRMydGIQY---RGYGQEIVETLA-EYAGVPVWN-GLTNEFHPTQLLADLLTMQEHLPGkaF 154

                         170       180
                  ....*....|....*....|.
gi 1361143906 158 SGKTVAIVGDiahsrvVHSNM 178
Cdd:PRK03515  155 NEMTLAYAGD------ARNNM 169
PRK04284 PRK04284
ornithine carbamoyltransferase; Provisional
 46-291 1.66e-09

ornithine carbamoyltransferase; Provisional


Pssm-ID: 235269 [Multi-domain]  Cd Length: 332  Bit Score: 57.83  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  46 RGRFAANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSSTAKGESLYDTVKTLASL--GVEvavIRHSDPEQVKALArQ 123
Cdd:PRK04284   44 KGKNIALIFEKDSTRTRCAFEVAAYDQGAHVTYLGPTGSQMGKKESTKDTARVLGGMydGIE---YRGFSQRTVETLA-E 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 124 EVGCKILNaGAGHWAHPTQALLDLYTMLKHFV-DLSGKTVAIVGDiAHSRVVHSNMWSLKRFGAHVILSGPQAMR-DRDC 201
Cdd:PRK04284  120 YSGVPVWN-GLTDEDHPTQVLADFLTAKEHLKkPYKDIKFTYVGD-GRNNVANALMQGAAIMGMDFHLVCPKELNpDDEL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 202 EQEAPYVP------------FEEALQTADVVMM-LRVQLERHQEkLFTSKQDYHKQYGLTLQRLRLMK-PEAIIMHPGP- 266
Cdd:PRK04284  198 LNKCKEIAaetggkititddIDEGVKGSDVIYTdVWVSMGEPDE-VWEERIKLLKPYQVNKEMMKKTGnPNAIFEHCLPs 276

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1361143906 267 FN----------------RGVEVADEVVEHPRSKIFEQKAN 291
Cdd:PRK04284  277 FHdldtkvgkeifekyglKEMEVTDEVFESKASVVFDEAEN 317
PRK07200 PRK07200
aspartate/ornithine carbamoyltransferase family protein; Validated
 20-288 6.47e-07

aspartate/ornithine carbamoyltransferase family protein; Validated


Pssm-ID: 235961 [Multi-domain]  Cd Length: 395  Bit Score: 50.12  E-value: 6.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  20 TLNELKAILARA---RYWEEN------WRPGMGpyrgrfaANLFFEPSTRTRFSFEVAEKKLGMEVVNFTPDVSSTAKGE 90
Cdd:PRK07200   30 TPDELKAVLDVAdalRALREEnistkvFNSGLG-------ISVFRDNSTRTRFSYASACNLLGLEVQDLDEGKSQIAHGE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906  91 SLYDTVkTLASLGVEVAVIR------------HSDPEQVKALARQEV----------GCKIlnagaghwAHPTQALLDLY 148
Cdd:PRK07200  103 TVRETA-NMISFMADVIGIRddmyigkgnaymREVGAAVDDGYKQGVlpqrptlvnlQCDI--------DHPTQSMADLL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 149 TMLKHFVD---LSGKTVAIVGDIAHS-----RVVHSNMWSLKRFGAHVILSGPQA---MRDRDCE----QEAPYVPF--- 210
Cdd:PRK07200  174 HLIEHFGGlenLKGKKIAMTWAYSPSygkplSVPQGIIGLMTRFGMDVTLAHPEGydlMPEVVEVakknAKASGGSFrqv 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 211 ---EEALQTADVV----------MMLRVQLERHQ--------EKLFTSKQDYHKQYGLTLQRLRLMKP-EAIIMHPGPFN 268
Cdd:PRK07200  254 nsmEEAFKDADIVypkswapykvMEERTELYRAGdhegikalEKELLAQNAQHKDWHCTEEMMKLTKDgKALYMHCLPAD 333

                         330       340
                  ....*....|....*....|....*.
gi 1361143906 269 -RGV-----EVADEVVEHPRSKIFEQ 288
Cdd:PRK07200  334 iSGVsckegEVTESVFDRYRIALYKE 359
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 155-276 4.47e-06

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 46.34  E-value: 4.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 155 VDLSGKTVAIV--GDIAhSRVvhsnMWSLKRFGAHVILSGPQAMRDRDCEQE-APYVPFEEALQTADVVMMLrVQLERHQ 231
Cdd:pfam02826  32 RELSGKTVGIIglGRIG-RAV----AKRLKAFGMKVIAYDRYPKPEEEEEELgARYVSLDELLAESDVVSLH-LPLTPET 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1361143906 232 EKLFTSKqdyhkqygltlqRLRLMKPEAIIMHPGpfnRGvEVADE 276
Cdd:pfam02826 106 RHLINAE------------RLALMKPGAILINTA---RG-GLVDE 134
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 155-261 9.51e-06

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240639 [Multi-domain]  Cd Length: 307  Bit Score: 46.29  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 155 VDLSGKTVAIVG---------DIAHSrvvhsnmwslkrFGAHVILSGPQAMRDRDceqeAPYVPFEEALQTADVVmMLRV 225
Cdd:cd12162   143 IELAGKTLGIIGygnigqavaRIARA------------FGMKVLFAERKGAPPLR----EGYVSLDELLAQSDVI-SLHC 205

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1361143906 226 QLERHQEKLFTSKqdyhkqygltlqRLRLMKPEAII 261
Cdd:cd12162   206 PLTPETRNLINAE------------ELAKMKPGAIL 229
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 156-261 8.52e-05

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 43.39  E-value: 8.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 156 DLSGKTVAIV--GDIAhSRVVHSnmwsLKRFGAHVILSGPQAMRDRDCEQEAPYVPFEEALQTADVVMMLrVQLERHQEK 233
Cdd:cd05198   137 ELEGKTVGIVglGRIG-QRVAKR----LQAFGMKVLYYDRTRKPEPEEDLGFRVVSLDELLAQSDVVVLH-LPLTPETRH 210

                          90       100
                  ....*....|....*....|....*...
gi 1361143906 234 LFTSKqdyhkqygltlqRLRLMKPEAII 261
Cdd:cd05198   211 LINEE------------ELALMKPGAVL 226
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
 143-276 2.17e-04

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 42.52  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 143 ALLDLYtmLKHFVDLSGKTVAIVGdIAH--SRVVHsnmwSLKRFGAHVILSGP-QAmrdrDCEQEAPYVPFEEALQTADV 219
Cdd:cd12158   101 ALLVLA--QRQGFSLKGKTVGIVG-VGNvgSRLAR----RLEALGMNVLLCDPpRA----EAEGDPGFVSLEELLAEADI 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 220 VmMLRVQLERHQEklftskqdyHKQYGL-TLQRLRLMKPEAIImhpgpFN--RGvEVADE 276
Cdd:cd12158   170 I-TLHVPLTRDGE---------HPTYHLlDEDFLAALKPGQIL-----INasRG-AVIDN 213
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 155-261 3.21e-04

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 41.70  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 155 VDLSGKTVAIV--GDIAHsRVVHsnmwSLKRFGAHVILSGPQAMRDRDCEQEAPYVPFEEALQTADVVMMlrvqlerHqe 232
Cdd:cd12172   138 TELYGKTLGIIglGRIGK-AVAR----RLSGFGMKVLAYDPYPDEEFAKEHGVEFVSLEELLKESDFISL-------H-- 203

                          90       100
                  ....*....|....*....|....*....
gi 1361143906 233 kLFTSKQDYHKqygLTLQRLRLMKPEAII 261
Cdd:cd12172   204 -LPLTPETRHL---INAAELALMKPGAIL 228
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 157-276 3.42e-04

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 41.50  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 157 LSGKTVAIVG------DIAHsrvvhsnmwSLKRFGAHVILSGPQAMrDRDCEQE--APYVPFEEALQTAD-VVMMLRVql 227
Cdd:cd12157   142 LDGKTVGILGmgalgrAIAR---------RLSGFGATLLYYDPHPL-DQAEEQAlnLRRVELDELLESSDfLVLALPL-- 209

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1361143906 228 erhqeklftSKQDYHKqygLTLQRLRLMKPEAIIMHPGpfnRGvEVADE 276
Cdd:cd12157   210 ---------TPDTLHL---INAEALAKMKPGALLVNPC---RG-SVVDE 242
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 155-260 6.17e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 41.02  E-value: 6.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 155 VDLSGKTVAIV--GDIAHsRVVHsnmwSLKRFGAHVILSGPQAMRD-RDCEQEAPYVPFEEALQTADVVmMLRVQLERHQ 231
Cdd:cd12175   138 RELSGKTVGIVglGNIGR-AVAR----RLRGFGVEVIYYDRFRDPEaEEKDLGVRYVELDELLAESDVV-SLHVPLTPET 211

                          90       100
                  ....*....|....*....|....*....
gi 1361143906 232 EKLFTSKqdyhkqygltlqRLRLMKPEAI 260
Cdd:cd12175   212 RHLIGAE------------ELAAMKPGAI 228
PRK13243 PRK13243
glyoxylate reductase; Reviewed
 155-263 6.83e-04

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 40.93  E-value: 6.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 155 VDLSGKTVAIVGdiaHSRVVHSNMWSLKRFGAHVILSgpQAMRDRDCEQE--APYVPFEEALQTADVVMmLRVQLerhqe 232
Cdd:PRK13243  146 YDVYGKTIGIIG---FGRIGQAVARRAKGFGMRILYY--SRTRKPEAEKElgAEYRPLEELLRESDFVS-LHVPL----- 214

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1361143906 233 klftSKQDYHKqygLTLQRLRLMKPEAIIMH 263
Cdd:PRK13243  215 ----TKETYHM---INEERLKLMKPTAILVN 238
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
 157-277 2.15e-03

Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240628 [Multi-domain]  Cd Length: 301  Bit Score: 39.06  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 157 LSGKTVAIVG---------DIAHSrvvhsnmwslkrFGAHVILSGPQAMRDRDCEQEAPYVPFEEALQTADVVmMLRVQL 227
Cdd:cd05303   137 LRGKTLGIIGfgrigrevaKIARA------------LGMNVIAYDPYPKDEQAVELGVKTVSLEELLKNSDFI-SLHVPL 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1361143906 228 ERHQEKLFTSKQdyhkqygltlqrLRLMKPEAIImhpgpFN--RGvEVADEV 277
Cdd:cd05303   204 TPETKHMINKKE------------LELMKDGAII-----INtsRG-GVIDEE 237
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 156-261 2.39e-03

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only]; Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 38.92  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 156 DLSGKTVAIVG---------DIAHSrvvhsnmwslkrFGAHVILSGPQAMRDRDcEQEAPYVPFEEALQTADVVmMLRVQ 226
Cdd:COG1052   140 DLSGKTLGIIGlgrigqavaRRAKG------------FGMKVLYYDRSPKPEVA-ELGAEYVSLDELLAESDIV-SLHCP 205

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1361143906 227 LerhqeklftSKQDYHKqygLTLQRLRLMKPEAII 261
Cdd:COG1052   206 L---------TPETRHL---INAEELALMKPGAIL 228
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 155-220 2.55e-03

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 39.02  E-value: 2.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1361143906 155 VDLSGKTVAIVG--DIAhSRVVHsnmwSLKRFGAHVILSGPQAMRDRDCEQEAPYV-PFEEALQTADVV 220
Cdd:COG0111   136 RELRGKTVGIVGlgRIG-RAVAR----RLRAFGMRVLAYDPSPKPEEAADLGVGLVdSLDELLAEADVV 199
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 154-220 3.00e-03

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 36.69  E-value: 3.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1361143906 154 FVDLSGKTVAIVG--DIAHSRVVHsnmwsLKRFGAHVILSGPQAmrDRDCEQEAPYVP--FEEALQTADVV 220
Cdd:pfam13241   2 FLDLRGKRVLVVGggEVAARKARK-----LLEAGAKVTVVSPEI--TPFLEGLLDLIRreFEGDLDGADLV 65
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 156-220 3.60e-03

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2-domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240659  Cd Length: 328  Bit Score: 38.58  E-value: 3.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361143906 156 DLSGKTVAIVG--DI--AHSRVvhsnmwsLKRFGAHVILSGPQamRDRDCEQE-APYVPFEEALQTADVV 220
Cdd:cd12183   141 DLHGKTVGVIGtgKIgqAFARI-------LKGFGCRVLAYDPY--PNPELAKLgVEYVDLDELLAESDII 201
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 155-220 7.96e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240655 [Multi-domain]  Cd Length: 317  Bit Score: 37.60  E-value: 7.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1361143906 155 VDLSGKTVAIVG------DIAHSrvvhsnmwsLKRFGAHVILSGP-QAMRDRDCEQEAPYVPFEEALQTADVV 220
Cdd:cd12178   140 HELAGKTLGIIGmgrigqAVARR---------AKAFGMKILYYNRhRLSEETEKELGATYVDLDELLKESDFV 203
 
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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