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Conserved domains on  [gi|1722882673|gb|TXD10236|]
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serine hydroxymethyltransferase [Staphylococcus haemolyticus]

Protein Classification

serine hydroxymethyltransferase( domain architecture ID 10011056)

serine hydroxymethyltransferase catalyzes the reversible, simultaneous conversions of L-serine to glycine (retro-aldol cleavage) and tetrahydrofolate to 5,10-methylenetetrahydrofolate (hydrolysis)

EC:  2.1.2.1
Gene Symbol:  glyA
Gene Ontology:  GO:0004372|GO:0030170|GO:0070905|GO:0008270|GO:0019264
PubMed:  12686103|2201683
SCOP:  4000675

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
 1-412 0e+00

serine hydroxymethyltransferase; Reviewed


:

Pssm-ID: 234571  Cd Length: 416  Bit Score: 828.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   1 MSYIQNQDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKA 80
Cdd:PRK00011    3 MDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  81 LFGAEHVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSPVNFSGKFYNFVDYGVDKETEKIDYEVVRQLAH 160
Cdd:PRK00011   83 LFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLAL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 161 EHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGGLILCK- 239
Cdd:PRK00011  163 EHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTNd 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 240 EEYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEGFRIVSGGTDNHLLSVDVKN 319
Cdd:PRK00011  243 EELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRS 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 320 SvNVTGKEAEATLDSIGITCNKNTIPFDQEKAFVTSGIRLGTPAATTRGFDEEAFKEVGRIISLALKNPNNDTKLKEARE 399
Cdd:PRK00011  323 K-GLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKE 401

                         410
                  ....*....|...
gi 1722882673 400 RVSRLTAKYPLYE 412
Cdd:PRK00011  402 EVKELCKRFPLYK 414
 
Name Accession Description Interval E-value
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
 1-412 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 828.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   1 MSYIQNQDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKA 80
Cdd:PRK00011    3 MDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  81 LFGAEHVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSPVNFSGKFYNFVDYGVDKETEKIDYEVVRQLAH 160
Cdd:PRK00011   83 LFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLAL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 161 EHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGGLILCK- 239
Cdd:PRK00011  163 EHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTNd 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 240 EEYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEGFRIVSGGTDNHLLSVDVKN 319
Cdd:PRK00011  243 EELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRS 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 320 SvNVTGKEAEATLDSIGITCNKNTIPFDQEKAFVTSGIRLGTPAATTRGFDEEAFKEVGRIISLALKNPNNDTKLKEARE 399
Cdd:PRK00011  323 K-GLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKE 401

                         410
                  ....*....|...
gi 1722882673 400 RVSRLTAKYPLYE 412
Cdd:PRK00011  402 EVKELCKRFPLYK 414
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
 1-412 0e+00

Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439882  Cd Length: 414  Bit Score: 822.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   1 MSYIQNQDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKA 80
Cdd:COG0112     2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  81 LFGAEHVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSPVNFSGKFYNFVDYGVDKETEKIDYEVVRQLAH 160
Cdd:COG0112    82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 161 EHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGGLILCKE 240
Cdd:COG0112   162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 241 EYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEGFRIVSGGTDNHLLSVDVKNS 320
Cdd:COG0112   242 ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 321 vNVTGKEAEATLDSIGITCNKNTIPFDQEKAFVTSGIRLGTPAATTRGFDEEAFKEVGRIISLALKNPNNDTKLKEARER 400
Cdd:COG0112   322 -GLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREE 400

                         410
                  ....*....|..
gi 1722882673 401 VSRLTAKYPLYE 412
Cdd:COG0112   401 VKELCKRFPLYP 412
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
 7-404 0e+00

Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.


Pssm-ID: 99733  Cd Length: 402  Bit Score: 654.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   7 QDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKALFGAEH 86
Cdd:cd00378     3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  87 VNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSP--VNFSGKFYNFVDYGVDKETEKIDYEVVRQLAHEHKP 164
Cdd:cd00378    83 ANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEFKP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 165 KLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGGLILC-KEEYK 243
Cdd:cd00378   163 KLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTrKGELA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 244 KDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEGFRIVSGGTDNHLLSVDVKNSvNV 323
Cdd:cd00378   243 KKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPK-GI 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 324 TGKEAEATLDSIGITCNKNTIPFDQEKAFVTSGIRLGTPAATTRGFDEEAFKEVGRIISLALKNPNNDTKLKEARERVSR 403
Cdd:cd00378   322 TGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVAE 401


                  .
gi 1722882673 404 L 404
Cdd:cd00378   402 L 402
SHMT pfam00464
Serine hydroxymethyltransferase;
4-381 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 615.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   4 IQNQDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKALFG 83
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  84 AE----HVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSPVNF-----SGKFYNFVDYGVDKETEKIDYEV 154
Cdd:pfam00464  81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 155 VRQLAHEHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGG 234
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 235 LILCK--------------EEYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEG 300
Cdd:pfam00464 241 MIFYRkgvksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 301 FRIVSGGTDNHLLSVDVKNSvNVTGKEAEATLDSIGITCNKNTIPFDqEKAFVTSGIRLGTPAATTRGFDEEAFKEVGRI 380
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPK-GLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGF 398


                  .
gi 1722882673 381 I 381
Cdd:pfam00464 399 I 399
 
Name Accession Description Interval E-value
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
 1-412 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 828.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   1 MSYIQNQDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKA 80
Cdd:PRK00011    3 MDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  81 LFGAEHVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSPVNFSGKFYNFVDYGVDKETEKIDYEVVRQLAH 160
Cdd:PRK00011   83 LFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLAL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 161 EHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGGLILCK- 239
Cdd:PRK00011  163 EHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTNd 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 240 EEYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEGFRIVSGGTDNHLLSVDVKN 319
Cdd:PRK00011  243 EELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRS 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 320 SvNVTGKEAEATLDSIGITCNKNTIPFDQEKAFVTSGIRLGTPAATTRGFDEEAFKEVGRIISLALKNPNNDTKLKEARE 399
Cdd:PRK00011  323 K-GLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKE 401

                         410
                  ....*....|...
gi 1722882673 400 RVSRLTAKYPLYE 412
Cdd:PRK00011  402 EVKELCKRFPLYK 414
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
 1-412 0e+00

Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439882  Cd Length: 414  Bit Score: 822.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   1 MSYIQNQDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKA 80
Cdd:COG0112     2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  81 LFGAEHVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSPVNFSGKFYNFVDYGVDKETEKIDYEVVRQLAH 160
Cdd:COG0112    82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 161 EHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGGLILCKE 240
Cdd:COG0112   162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 241 EYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEGFRIVSGGTDNHLLSVDVKNS 320
Cdd:COG0112   242 ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSK 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 321 vNVTGKEAEATLDSIGITCNKNTIPFDQEKAFVTSGIRLGTPAATTRGFDEEAFKEVGRIISLALKNPNNDTKLKEARER 400
Cdd:COG0112   322 -GLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREE 400

                         410
                  ....*....|..
gi 1722882673 401 VSRLTAKYPLYE 412
Cdd:COG0112   401 VKELCKRFPLYP 412
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
 1-411 0e+00

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 694.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   1 MSYIQNQDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKA 80
Cdd:PRK13034    6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  81 LFGAEHVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSPVNFSGKFYNFVDYGVDKETEKIDYEVVRQLAH 160
Cdd:PRK13034   86 LFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVEELAK 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 161 EHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGGLILCK- 239
Cdd:PRK13034  166 EHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNd 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 240 EEYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEGFRIVSGGTDNHLLSVDVKN 319
Cdd:PRK13034  246 EEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRP 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 320 SvNVTGKEAEATLDSIGITCNKNTIPFDQEKAFVTSGIRLGTPAATTRGFDEEAFKEVGRIISLALKNPNNDTKLKEARE 399
Cdd:PRK13034  326 K-GLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRK 404

                         410
                  ....*....|..
gi 1722882673 400 RVSRLTAKYPLY 411
Cdd:PRK13034  405 EVKALCSRFPIY 416
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
 7-404 0e+00

Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.


Pssm-ID: 99733  Cd Length: 402  Bit Score: 654.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   7 QDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKALFGAEH 86
Cdd:cd00378     3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  87 VNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSP--VNFSGKFYNFVDYGVDKETEKIDYEVVRQLAHEHKP 164
Cdd:cd00378    83 ANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEFKP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 165 KLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGGLILC-KEEYK 243
Cdd:cd00378   163 KLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTrKGELA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 244 KDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEGFRIVSGGTDNHLLSVDVKNSvNV 323
Cdd:cd00378   243 KKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPK-GI 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 324 TGKEAEATLDSIGITCNKNTIPFDQEKAFVTSGIRLGTPAATTRGFDEEAFKEVGRIISLALKNPNNDTKLKEARERVSR 403
Cdd:cd00378   322 TGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVAE 401


                  .
gi 1722882673 404 L 404
Cdd:cd00378   402 L 402
SHMT pfam00464
Serine hydroxymethyltransferase;
4-381 0e+00

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 615.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   4 IQNQDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKALFG 83
Cdd:pfam00464   1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  84 AE----HVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSPVNF-----SGKFYNFVDYGVDKETEKIDYEV 154
Cdd:pfam00464  81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 155 VRQLAHEHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGG 234
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 235 LILCK--------------EEYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEG 300
Cdd:pfam00464 241 MIFYRkgvksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 301 FRIVSGGTDNHLLSVDVKNSvNVTGKEAEATLDSIGITCNKNTIPFDqEKAFVTSGIRLGTPAATTRGFDEEAFKEVGRI 380
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPK-GLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGF 398


                  .
gi 1722882673 381 I 381
Cdd:pfam00464 399 I 399
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
 4-386 1.32e-180

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 510.29  E-value: 1.32e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   4 IQNQDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKALFG 83
Cdd:PTZ00094   15 LKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  84 AEH----VNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHG-----SPVNFSGKFYNFVDYGVDKETEkIDYEV 154
Cdd:PTZ00094   95 LDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEKGL-IDYDK 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 155 VRQLAHEHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGG 234
Cdd:PTZ00094  174 LEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSG 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 235 LILCKEEYKKD----IDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEGFRIVSGGTDN 310
Cdd:PTZ00094  254 LIFYRKKVKPDienkINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGTDN 333

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1722882673 311 HLLSVDVKnSVNVTGKEAEATLDSIGITCNKNTIPFDQEkAFVTSGIRLGTPAATTRGFDEEAFKEVGRIISLALK 386
Cdd:PTZ00094  334 HLVLVDLR-PFGITGSKMEKLLDAVNISVNKNTIPGDKS-ALNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVK 407
PRK13580 PRK13580
glycine hydroxymethyltransferase;
4-411 1.18e-175

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 499.57  E-value: 1.18e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   4 IQNQDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKALFG 83
Cdd:PRK13580   30 ILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  84 AEHVNVQPHSGSQANMAVYLVAL------------------------------EMGDTV-LGMNLSHGGHLTHGSPVNFS 132
Cdd:PRK13580  110 AEHAYVQPHSGADANLVAFWAILahkvespaleklgaktvndlteedwealraELGNQRlLGMSLDSGGHLTHGFRPNIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 133 GKFYNFVDYGVDKETEKIDYEVVRQLAHEHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGL--- 209
Cdd:PRK13580  190 GKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVftg 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 210 HPNPVEHADFVTTTTHKTLRGPRGGLILCKEEYKKDIDKTIfPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNA 289
Cdd:PRK13580  270 DEDPVPHADIVTTTTHKTLRGPRGGLVLAKKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNA 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 290 KVLSQTLQEEGFRIVSGGTDNHLLSVDVkNSVNVTGKEAEATLDSIGITCNKNTIPFDQEKAFVTSGIRLGTPAATTRGF 369
Cdd:PRK13580  349 RALAEGFLKRGARLVTGGTDNHLVLIDV-TSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTLGM 427

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1722882673 370 DEEAFKEVGRIISLALKN-------PNNDTKLK---------EARERVSRLTAKYPLY 411
Cdd:PRK13580  428 GSDEMDEVAELIVKVLSNttpgttaEGAPSKAKyeldegvaqEVRARVAELLARFPLY 485
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
 7-399 1.22e-157

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 452.90  E-value: 1.22e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   7 QDKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKALFGAEH 86
Cdd:PLN03226   18 VDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFRLDP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  87 ----VNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHG-----SPVNFSGKFYNFVDYGVDKETEKIDYEVVRQ 157
Cdd:PLN03226   98 ekwgVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtdgKKISATSIYFESMPYRLDESTGLIDYDKLEK 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 158 LAHEHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGGLIL 237
Cdd:PLN03226  178 KAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGGMIF 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 238 CKE--------------EYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEGFRI 303
Cdd:PLN03226  258 FRKgpkppkgqgegavyDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSKGYKL 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 304 VSGGTDNHLLSVDVKNsVNVTGKEAEATLDSIGITCNKNTIPFDQEkAFVTSGIRLGTPAATTRGFDEEAFKEVG----R 379
Cdd:PLN03226  338 VTGGTDNHLVLWDLRP-LGLTGSRVEKVLDLAHITLNKNAVPGDSS-ALVPGGVRIGTPAMTSRGLVEKDFEKVAeflhR 415

                         410       420
                  ....*....|....*....|.
gi 1722882673 380 IISLALK-NPNNDTKLKEARE 399
Cdd:PLN03226  416 AVTIALKiQKEHGKKLKDFKK 436
PLN02271 PLN02271
serine hydroxymethyltransferase
 8-401 4.51e-112

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 340.24  E-value: 4.51e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673   8 DKAVYEAIQNEYNRQNNNIELIASENFVSEAVMEAQGSVMTNKYAEGYPGRRYYGGCDYVDVTETIAIERAKALFGAEH- 86
Cdd:PLN02271  133 DPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFGLDSe 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  87 ---VNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHG--SP----VNFSGKFYNFVDYGVDKETEKIDYEVVRQ 157
Cdd:PLN02271  213 kwgVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyyTPggkkVSGASIFFESLPYKVNPQTGYIDYDKLEE 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 158 LAHEHKPKLIVAGTSAYSRQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTLRGPRGGLIL 237
Cdd:PLN02271  293 KALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRGGIIF 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 238 CKE--------------------EYKKDIDKTIFPGIQGGPLEHVIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQ 297
Cdd:PLN02271  373 YRKgpklrkqgmllshgddnshyDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALASALL 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 298 EEGFRIVSGGTDNHLLSVDVKNsVNVTGKEAEATLDSIGITCNKNTIpFDQEKAFVTSGIRLGTPAATTRGFDEEAF--- 374
Cdd:PLN02271  453 RRKCRLVTGGTDNHLLLWDLTT-LGLTGKNYEKVCEMCHITLNKTAI-FGDNGTISPGGVRIGTPAMTSRGCLESDFeti 530

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1722882673 375 ---------------KEVGRIISLALKNPNNDTKLKEARERV 401
Cdd:PLN02271  531 adfllraaqiasavqREHGKLQKEFLKGLQNNKDIVELRNRV 572
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 74-236 2.03e-24

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 98.61  E-value: 2.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  74 AIERAKALF--GAEHVNVQPhSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSPVnfsgKFYNFVDYGVDKETE-KI 150
Cdd:cd01494     5 LEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAEL----AGAKPVPVPVDDAGYgGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 151 DYEVVRQLAHEHKPKLIVAGTSAYSR--QLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPNPVEHADFVTTTTHKTL 228
Cdd:cd01494    80 DVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNL 159


                  ....*...
gi 1722882673 229 RGPRGGLI 236
Cdd:cd01494   160 GGEGGGVV 167
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
34-304 1.21e-06

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 50.00  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  34 FVSEAVMEAqgsvmtNKYAEGYPGRRYYGGCD-YVDVTETIAierakALFGAEHV-------NVQPHSGSQANM-AVYLV 104
Cdd:pfam00155  14 DTLPAVAKA------EKDALAGGTRNLYGPTDgHPELREALA-----KFLGRSPVlkldreaAVVFGSGAGANIeALIFL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 105 ALEMGDTVLGMNLSHGGHLT----HGSPVnfsgKFYNFVDygvdKETEKIDYEVVRQlAHEHKPKLIVAGT------SAY 174
Cdd:pfam00155  83 LANPGDAILVPAPTYASYIRiarlAGGEV----VRYPLYD----SNDFHLDFDALEA-ALKEKPKVVLHTSphnptgTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 175 SRQlDFKKFKEIADEVGAKLMVDMAHiAGLVAAGLHPNPV------EHADFVTTTTHKT--LRGPRGGLILCKEEYKKDI 246
Cdd:pfam00155 154 TLE-ELEKLLDLAKEHNILLLVDEAY-AGFVFGSPDAVATrallaeGPNLLVVGSFSKAfgLAGWRVGYILGNAAVISQL 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1722882673 247 DKTIFPGIQGGPLEHvIAAKAVAFGEALEQDFKVYQEQVIKNAKVLSQTLQEEGFRIV 304
Cdd:pfam00155 232 RKLARPFYSSTHLQA-AAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVL 288
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 153-311 1.38e-06

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 49.87  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 153 EVVRQLAHEHKPKLIVA-------GTSAysrqlDFKKFKEIADEVGAKLMVDMAHIAGLV---AAGLHPNPVEHA--DFV 220
Cdd:cd06454   122 KLLREARRPYGKKLIVTegvysmdGDIA-----PLPELVDLAKKYGAILFVDEAHSVGVYgphGRGVEEFGGLTDdvDII 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 221 TTTTHKTLrGPRGGLILCKEEYkkdIDK-------TIFpgiQGGPLEHVIAAKAVAFGEALEQDFKVyqEQVIKNAKVLS 293
Cdd:cd06454   197 MGTLGKAF-GAVGGYIAGSKEL---IDYlrsyargFIF---STSLPPAVAAAALAALEVLQGGPERR--ERLQENVRYLR 267

                         170
                  ....*....|....*...
gi 1722882673 294 QTLQEEGFRIvsGGTDNH 311
Cdd:cd06454   268 RGLKELGFPV--GGSPSH 283
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
151-305 1.02e-05

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 47.31  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 151 DYEVVRQLAHEHKPKLIVAgTSAYSRQLDF---KKFKEIADEVGAKLMVDMAHI--------AGLVAA-GLhpnpVEHAD 218
Cdd:PRK07179  169 DVDHLRRQIERHGPGIIVV-DSVYSTTGTIaplADIVDIAEEFGCVLVVDESHSlgthgpqgAGLVAElGL----TSRVH 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 219 FVTTTTHKTLRGpRGGLILCKEEYKKDIDKTIFPGI-QGGPLEHVIAakavAFGEALE----QDFKvyQEQVIKNAKVLS 293
Cdd:PRK07179  244 FITASLAKAFAG-RAGIITCPRELAEYVPFVSYPAIfSSTLLPHEIA----GLEATLEviesADDR--RARLHANARFLR 316

                         170
                  ....*....|..
gi 1722882673 294 QTLQEEGFRIVS 305
Cdd:PRK07179  317 EGLSELGYNIRS 328
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 74-228 1.78e-05

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 46.09  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  74 AIERAKALFGAEHVNVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGH-----LTHGSPVnfsgkfynFVDYGVDKETE 148
Cdd:cd00615    64 AQELAARAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVinglvLSGAVPV--------YLKPERNPYYG 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 149 KI----DYEVVRQLAHEHKPKLIVA------GTSAysrqlDFKKFKEIADEVGAKLMVDMAHIAglvAAGLHPNPVEH-- 216
Cdd:cd00615   136 IAggipPETFKKALIEHPDAKAAVItnptyyGICY-----NLRKIVEEAHHRGLPVLVDEAHGA---HFRFHPILPSSaa 207

                         170
                  ....*....|....*
gi 1722882673 217 ---ADFVTTTTHKTL 228
Cdd:cd00615   208 magADIVVQSTHKTL 222
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
76-242 1.66e-04

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 42.97  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673  76 ERAKALFGAEHVnVQPHSGSQANMAVYLVALEMGDTVLGMNLSHGGHLTHGSPVNFSGKFYNFVDygvDKETEKIDYEVV 155
Cdd:pfam01212  39 DRVAELFGKEAA-LFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETGGHAELGGVQPRPLD---GDEAGNMDLEDL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 156 RQLAHEH------KPKLIV-------AGTSAYSRQlDFKKFKEIADEVGAKLMVDMAHIA-GLVAAGLHPNPV-EHADFV 220
Cdd:pfam01212 115 EAAIREVgadifpPTGLISlenthnsAGGQVVSLE-NLREIAALAREHGIPVHLDGARFAnAAVALGVIVKEItSYADSV 193

                         170       180
                  ....*....|....*....|..
gi 1722882673 221 TTTTHKTLRGPRGGLILCKEEY 242
Cdd:pfam01212 194 TMCLSKGLGAPVGSVLAGSDDF 215
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
146-337 4.92e-04

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 42.05  E-value: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 146 ETEKIDYEVVRQLAHEhKPKLI-------VAGTsaysrQLDFKKFKEIADEVGAKLMVDMAHIAGLVAAGLHPnpvEHAD 218
Cdd:COG0520   138 EDGELDLEALEALLTP-RTKLVavthvsnVTGT-----VNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQA---LGCD 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 219 FVTTTTHKtLRGPR--GGLILCKEEYKKD---------IDKTIFPGIQGGPLEHV-------IAAkAVAFGEALEqdfkv 280
Cdd:COG0520   209 FYAFSGHK-LYGPTgiGVLYGKRELLEALppflggggmIEWVSFDGTTYADLPRRfeagtpnIAG-AIGLGAAID----- 281

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722882673 281 YQEQV-IKN--------AKVLSQTLQE-EGFRIVSGGTDNHLLSVdvkNSVNVTGKEAE---ATLDSIGI 337
Cdd:COG0520   282 YLEAIgMEAiearerelTAYALEGLAAiPGVRILGPADPEDRSGI---VSFNVDGVHPHdvaALLDDEGI 348
 
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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