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Conserved domains on  [gi|851341915|ref|WP_048188941|]
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serine hydroxymethyltransferase [Candidatus Nitrosotenuis cloacae]

Protein Classification

serine hydroxymethyltransferase( domain architecture ID 10000611)

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
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 COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
4-421 1.38e-180

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: 509.96  E-value: 1.38e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915   4 SATKASYKKILSDLQEHNKWFENSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKL 83
Cdd:COG0112    3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  84 YKAKFADVRPISGVVANLAVYSAFTNPGDVMIAPSIPAGGHISHGKKehsGTAGlVHGLDIEFYPFDADEMTIDVDKTKA 163
Cdd:COG0112   83 FGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSP---VNFS-GKGYNVVSYGVDPETGLIDYDEVRK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 164 KVEELKaanrlPKMAMFGGSLFLFPHPVKELSDFLKGYNIHINYDAAHVAGLIAGGQFQDPLrEGADTMTMSTHKTLFGP 243
Cdd:COG0112  159 LALEHK-----PKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPV-PGADVVTTTTHKTLRGP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 244 QGGLVLGREEHAEPIKKATFPGLTSSHHIHHMAAKAIAFAEALEFG-KQYAKDVIKNAKALADALSDAGFKVLGekrGYT 322
Cdd:COG0112  233 RGGLILCNEELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEfKEYAKQVVKNAKALAEALAERGFRVVS---GGT 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 323 KSHQIAVNVLDYSDGGK-VEADLEKANIIVNRQLIPGDIkagRNYFHPGGIRLGVSELTRLGMKSAEMKEIAGYIKNIVI 401
Cdd:COG0112  310 DNHLVLVDLRSKGLTGKeAEKALERAGITVNKNAIPFDP---RSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLD 386
                        410       420
                 ....*....|....*....|...
gi 851341915 402 EKKDP---KKLAAKVKSFRKDYQ 421
Cdd:COG0112  387 NPEDEavlAEVREEVKELCKRFP 409
 
Name Accession Description Interval E-value
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
4-421 1.38e-180

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: 509.96  E-value: 1.38e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915   4 SATKASYKKILSDLQEHNKWFENSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKL 83
Cdd:COG0112    3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  84 YKAKFADVRPISGVVANLAVYSAFTNPGDVMIAPSIPAGGHISHGKKehsGTAGlVHGLDIEFYPFDADEMTIDVDKTKA 163
Cdd:COG0112   83 FGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSP---VNFS-GKGYNVVSYGVDPETGLIDYDEVRK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 164 KVEELKaanrlPKMAMFGGSLFLFPHPVKELSDFLKGYNIHINYDAAHVAGLIAGGQFQDPLrEGADTMTMSTHKTLFGP 243
Cdd:COG0112  159 LALEHK-----PKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPV-PGADVVTTTTHKTLRGP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 244 QGGLVLGREEHAEPIKKATFPGLTSSHHIHHMAAKAIAFAEALEFG-KQYAKDVIKNAKALADALSDAGFKVLGekrGYT 322
Cdd:COG0112  233 RGGLILCNEELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEfKEYAKQVVKNAKALAEALAERGFRVVS---GGT 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 323 KSHQIAVNVLDYSDGGK-VEADLEKANIIVNRQLIPGDIkagRNYFHPGGIRLGVSELTRLGMKSAEMKEIAGYIKNIVI 401
Cdd:COG0112  310 DNHLVLVDLRSKGLTGKeAEKALERAGITVNKNAIPFDP---RSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLD 386
                        410       420
                 ....*....|....*....|...
gi 851341915 402 EKKDP---KKLAAKVKSFRKDYQ 421
Cdd:COG0112  387 NPEDEavlAEVREEVKELCKRFP 409
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
17-426 1.63e-168

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 479.57  E-value: 1.63e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  17 LQEHNKWFENSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKLYKAKFADVRPISG 96
Cdd:PRK00011  17 IEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELFGAEYANVQPHSG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  97 VVANLAVYSAFTNPGDVMIAPSIPAGGHISHGKKehSGTAGLvhGLDIEFYPFDADEMTIDVDKTKAKVEELKaanrlPK 176
Cdd:PRK00011  97 SQANAAVYFALLKPGDTILGMDLAHGGHLTHGSP--VNFSGK--LYNVVSYGVDEETGLIDYDEVEKLALEHK-----PK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 177 MAMFGGSLFLFPHPVKELSDFLKGYNIHINYDAAHVAGLIAGGQFQDPLReGADTMTMSTHKTLFGPQGGLVLGR-EEHA 255
Cdd:PRK00011 168 LIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVP-HADVVTTTTHKTLRGPRGGLILTNdEELA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 256 EPIKKATFPGLTSSHHIHHMAAKAIAFAEALEFG-KQYAKDVIKNAKALADALSDAGFKVLGekrGYTKSHQIAVNVLDY 334
Cdd:PRK00011 247 KKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEfKEYAQQVVKNAKALAEALAERGFRVVS---GGTDNHLVLVDLRSK 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 335 SDGGK-VEADLEKANIIVNRQLIPGDikaGRNYFHPGGIRLGVSELTRLGMKSAEMKEIAGYIKNIVI---EKKDPKKLA 410
Cdd:PRK00011 324 GLTGKeAEAALEEANITVNKNAVPFD---PRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDnpdDEAVIEEVK 400
                        410
                 ....*....|....*.
gi 851341915 411 AKVKSFRKDYQKVHYC 426
Cdd:PRK00011 401 EEVKELCKRFPLYKYL 416
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
11-416 3.53e-146

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: 422.00  E-value: 3.53e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  11 KKILSDLQEHNKWFENSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKLYKAKFAD 90
Cdd:cd00378    5 PEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEYAN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  91 VRPISGVVANLAVYSAFTNPGDVMIAPSIPAGGHISHGKKehsGTAGLVHGLDIEF-YPFDADEMTIDVDKTKAKVEELK 169
Cdd:cd00378   85 VQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSF---TKVSASGKLFESVpYGVDPETGLIDYDALEKMALEFK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 170 aanrlPKMAMFGGSLFLFPHPVKELSDFLKGYNIHINYDAAHVAGLIAGGQFQDPLReGADTMTMSTHKTLFGPQGGLVL 249
Cdd:cd00378  162 -----PKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLP-GADVVTTTTHKTLRGPRGGLIL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 250 GR-EEHAEPIKKATFPGLTSSHHIHHMAAKAIAFAEALE-FGKQYAKDVIKNAKALADALSDAGFKVLGEKRGytkSHQI 327
Cdd:cd00378  236 TRkGELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEpEFKAYAKQVVENAKALAEALKERGFKVVSGGTD---NHLV 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 328 AVNVLDYS-DGGKVEADLEKANIIVNRQLIPGDIKAGrnyFHPGGIRLGVSELTRLGMKSAEMKEIAGYIKNIVIEKKD- 405
Cdd:cd00378  313 LVDLRPKGiTGKAAEDALEEAGITVNKNTLPWDPSSP---FVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDv 389
                        410
                 ....*....|...
gi 851341915 406 --PKKLAAKVKSF 416
Cdd:cd00378  390 avAEEVRKEVAEL 402
SHMT pfam00464
Serine hydroxymethyltransferase;
25-396 1.14e-83

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 262.38  E-value: 1.14e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915   25 ENSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKLYKAK----FADVRPISGVVAN 100
Cdd:pfam00464  20 REGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLDpakwGVNVQPLSGSPAN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  101 LAVYSAFTNPGDVMIAPSIPAGGHISHGKKEHSGTAGLVhGLDIEFYPFDADEMT--IDVDKTKAKVEELKaanrlPKMA 178
Cdd:pfam00464 100 LAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISAS-SKFFESMPYGVDPETgyIDYDQLEKNAKLFR-----PKLI 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  179 MFGGS----LFLFPHpVKELSDFLKGYnihINYDAAHVAGLIAGGQFQDPLrEGADTMTMSTHKTLFGPQGGLVLGR--- 251
Cdd:pfam00464 174 VAGTSaysrLIDYAR-FREIADEVGAY---LMVDMAHISGLVAAGVIPSPF-PYADVVTTTTHKTLRGPRGGMIFYRkgv 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  252 -----------EEHAEPIKKATFPGLTSSHHIHHMAAKAIAFAEAL--EFgKQYAKDVIKNAKALADALSDAGFKVLGek 318
Cdd:pfam00464 249 ksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALtpEF-KEYQQQVVKNAKALAEALTERGYKLVS-- 325
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851341915  319 rGYTKSHQIAVNVLDYS-DGGKVEADLEKANIIVNRQLIPGDIKAgrnyFHPGGIRLGVSELTRLGMKSAEMKEIAGYI 396
Cdd:pfam00464 326 -GGTDNHLVLVDLRPKGlDGARAEKVLEAANITANKNTIPGDKSA----FVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
 
Name Accession Description Interval E-value
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
4-421 1.38e-180

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: 509.96  E-value: 1.38e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915   4 SATKASYKKILSDLQEHNKWFENSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKL 83
Cdd:COG0112    3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  84 YKAKFADVRPISGVVANLAVYSAFTNPGDVMIAPSIPAGGHISHGKKehsGTAGlVHGLDIEFYPFDADEMTIDVDKTKA 163
Cdd:COG0112   83 FGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSP---VNFS-GKGYNVVSYGVDPETGLIDYDEVRK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 164 KVEELKaanrlPKMAMFGGSLFLFPHPVKELSDFLKGYNIHINYDAAHVAGLIAGGQFQDPLrEGADTMTMSTHKTLFGP 243
Cdd:COG0112  159 LALEHK-----PKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPV-PGADVVTTTTHKTLRGP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 244 QGGLVLGREEHAEPIKKATFPGLTSSHHIHHMAAKAIAFAEALEFG-KQYAKDVIKNAKALADALSDAGFKVLGekrGYT 322
Cdd:COG0112  233 RGGLILCNEELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEfKEYAKQVVKNAKALAEALAERGFRVVS---GGT 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 323 KSHQIAVNVLDYSDGGK-VEADLEKANIIVNRQLIPGDIkagRNYFHPGGIRLGVSELTRLGMKSAEMKEIAGYIKNIVI 401
Cdd:COG0112  310 DNHLVLVDLRSKGLTGKeAEKALERAGITVNKNAIPFDP---RSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLD 386
                        410       420
                 ....*....|....*....|...
gi 851341915 402 EKKDP---KKLAAKVKSFRKDYQ 421
Cdd:COG0112  387 NPEDEavlAEVREEVKELCKRFP 409
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
17-426 1.63e-168

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 479.57  E-value: 1.63e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  17 LQEHNKWFENSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKLYKAKFADVRPISG 96
Cdd:PRK00011  17 IEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKELFGAEYANVQPHSG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  97 VVANLAVYSAFTNPGDVMIAPSIPAGGHISHGKKehSGTAGLvhGLDIEFYPFDADEMTIDVDKTKAKVEELKaanrlPK 176
Cdd:PRK00011  97 SQANAAVYFALLKPGDTILGMDLAHGGHLTHGSP--VNFSGK--LYNVVSYGVDEETGLIDYDEVEKLALEHK-----PK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 177 MAMFGGSLFLFPHPVKELSDFLKGYNIHINYDAAHVAGLIAGGQFQDPLReGADTMTMSTHKTLFGPQGGLVLGR-EEHA 255
Cdd:PRK00011 168 LIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVP-HADVVTTTTHKTLRGPRGGLILTNdEELA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 256 EPIKKATFPGLTSSHHIHHMAAKAIAFAEALEFG-KQYAKDVIKNAKALADALSDAGFKVLGekrGYTKSHQIAVNVLDY 334
Cdd:PRK00011 247 KKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEfKEYAQQVVKNAKALAEALAERGFRVVS---GGTDNHLVLVDLRSK 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 335 SDGGK-VEADLEKANIIVNRQLIPGDikaGRNYFHPGGIRLGVSELTRLGMKSAEMKEIAGYIKNIVI---EKKDPKKLA 410
Cdd:PRK00011 324 GLTGKeAEAALEEANITVNKNAVPFD---PRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDnpdDEAVIEEVK 400
                        410
                 ....*....|....*.
gi 851341915 411 AKVKSFRKDYQKVHYC 426
Cdd:PRK00011 401 EEVKELCKRFPLYKYL 416
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
11-416 3.53e-146

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: 422.00  E-value: 3.53e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  11 KKILSDLQEHNKWFENSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKLYKAKFAD 90
Cdd:cd00378    5 PEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEYAN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  91 VRPISGVVANLAVYSAFTNPGDVMIAPSIPAGGHISHGKKehsGTAGLVHGLDIEF-YPFDADEMTIDVDKTKAKVEELK 169
Cdd:cd00378   85 VQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSF---TKVSASGKLFESVpYGVDPETGLIDYDALEKMALEFK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 170 aanrlPKMAMFGGSLFLFPHPVKELSDFLKGYNIHINYDAAHVAGLIAGGQFQDPLReGADTMTMSTHKTLFGPQGGLVL 249
Cdd:cd00378  162 -----PKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLP-GADVVTTTTHKTLRGPRGGLIL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 250 GR-EEHAEPIKKATFPGLTSSHHIHHMAAKAIAFAEALE-FGKQYAKDVIKNAKALADALSDAGFKVLGEKRGytkSHQI 327
Cdd:cd00378  236 TRkGELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEpEFKAYAKQVVENAKALAEALKERGFKVVSGGTD---NHLV 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 328 AVNVLDYS-DGGKVEADLEKANIIVNRQLIPGDIKAGrnyFHPGGIRLGVSELTRLGMKSAEMKEIAGYIKNIVIEKKD- 405
Cdd:cd00378  313 LVDLRPKGiTGKAAEDALEEAGITVNKNTLPWDPSSP---FVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDv 389
                        410
                 ....*....|...
gi 851341915 406 --PKKLAAKVKSF 416
Cdd:cd00378  390 avAEEVRKEVAEL 402
SHMT pfam00464
Serine hydroxymethyltransferase;
25-396 1.14e-83

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 262.38  E-value: 1.14e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915   25 ENSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKLYKAK----FADVRPISGVVAN 100
Cdd:pfam00464  20 REGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLDpakwGVNVQPLSGSPAN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  101 LAVYSAFTNPGDVMIAPSIPAGGHISHGKKEHSGTAGLVhGLDIEFYPFDADEMT--IDVDKTKAKVEELKaanrlPKMA 178
Cdd:pfam00464 100 LAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISAS-SKFFESMPYGVDPETgyIDYDQLEKNAKLFR-----PKLI 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  179 MFGGS----LFLFPHpVKELSDFLKGYnihINYDAAHVAGLIAGGQFQDPLrEGADTMTMSTHKTLFGPQGGLVLGR--- 251
Cdd:pfam00464 174 VAGTSaysrLIDYAR-FREIADEVGAY---LMVDMAHISGLVAAGVIPSPF-PYADVVTTTTHKTLRGPRGGMIFYRkgv 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  252 -----------EEHAEPIKKATFPGLTSSHHIHHMAAKAIAFAEAL--EFgKQYAKDVIKNAKALADALSDAGFKVLGek 318
Cdd:pfam00464 249 ksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALtpEF-KEYQQQVVKNAKALAEALTERGYKLVS-- 325
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851341915  319 rGYTKSHQIAVNVLDYS-DGGKVEADLEKANIIVNRQLIPGDIKAgrnyFHPGGIRLGVSELTRLGMKSAEMKEIAGYI 396
Cdd:pfam00464 326 -GGTDNHLVLVDLRPKGlDGARAEKVLEAANITANKNTIPGDKSA----FVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
25-416 1.67e-80

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 254.50  E-value: 1.67e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  25 ENSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKLYKAKFADVRPISGVVANLAVY 104
Cdd:PRK13034  28 QDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQLFGCDYANVQPHSGSQANGAVY 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 105 SAFTNPGDVMIAPSIPAGGHISHGKKEhSGTAGLVHGLdieFYPFDADEMTIDVDktkaKVEELKAANRlPKMAMFGGSL 184
Cdd:PRK13034 108 LALLKPGDTILGMSLSHGGHLTHGAKV-SLSGKWYNAV---QYGVDRLTGLIDYD----EVEELAKEHK-PKLIIAGFSA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 185 FlfphpVKELsDFLKGYNI------HINYDAAHVAGLIAGGQFQDPLrEGADTMTMSTHKTLFGPQGGLVLGR-EEHAEP 257
Cdd:PRK13034 179 Y-----PREL-DFARFREIadevgaLLMVDMAHIAGLVAAGEHPNPF-PHAHVVTTTTHKTLRGPRGGMILTNdEEIAKK 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 258 IKKATFPGLTSSHHIHHMAAKAIAFAEALEFG-KQYAKDVIKNAKALADALSDAGFKVLGekrGYTKSHQIAVNVLDYSD 336
Cdd:PRK13034 252 INSAVFPGLQGGPLMHVIAAKAVAFGEALQPEfKTYAKQVIANAQALAEVLKERGYDLVS---GGTDNHLLLVDLRPKGL 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 337 GGK-VEADLEKANIIVNRQLIPGDIkagRNYFHPGGIRLGVSELTRLGMKSAEMKEIAGYI-------KNIVIEKKDPKK 408
Cdd:PRK13034 329 SGKdAEQALERAGITVNKNTVPGDT---ESPFVTSGIRIGTPAGTTRGFGEAEFREIANWIldvlddlGNAALEQRVRKE 405

                 ....*...
gi 851341915 409 LAAKVKSF 416
Cdd:PRK13034 406 VKALCSRF 413
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
26-418 3.67e-73

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 236.80  E-value: 3.67e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  26 NSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKLYKAKF----ADVRPISGVVANL 101
Cdd:PTZ00094  35 EGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFGLDPeewgVNVQPYSGSPANF 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 102 AVYSAFTNPGDVMIAPSIPAGGHISHG----KKEHSGTAglvHGLDIEFYPFDADEMtIDVDktkaKVEELKAANRlPKM 177
Cdd:PTZ00094 115 AVYTALLQPHDRIMGLDLPSGGHLTHGfytaKKKVSATS---IYFESLPYQVNEKGL-IDYD----KLEELAKAFR-PKL 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 178 AMFGGSLFlfphP-------VKELSDFLKGYnihINYDAAHVAGLIAGGQFQDPLrEGADTMTMSTHKTLFGPQGGLVL- 249
Cdd:PTZ00094 186 IIAGASAY----PrdidykrFREICDSVGAY---LMADIAHTSGLVAAGVLPSPF-PYADVVTTTTHKSLRGPRSGLIFy 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 250 ---GREEHAEPIKKATFPGLTSSHHIHHMAAKAIAFAEAL--EFgKQYAKDVIKNAKALADALSDAGFKVLGekrGYTKS 324
Cdd:PTZ00094 258 rkkVKPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQspEW-KEYAKQVLKNAKALAAALEKRGYDLVT---GGTDN 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 325 HQIAVNVLDYS-DGGKVEADLEKANIIVNRQLIPGDIKAgrnyFHPGGIRLGVSELTRLGMKSAEMKEIAGYIKNIV--- 400
Cdd:PTZ00094 334 HLVLVDLRPFGiTGSKMEKLLDAVNISVNKNTIPGDKSA----LNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVkla 409
                        410       420
                 ....*....|....*....|
gi 851341915 401 --IEKKDPKKLAAKVKSFRK 418
Cdd:PTZ00094 410 qeIQKQVGKKLVDFKKALEK 429
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
14-418 8.74e-63

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 210.22  E-value: 8.74e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  14 LSDLQEHNK---WfeNSIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKLYKAKFA- 89
Cdd:PLN03226  22 IADIIEKEKrrqW--KGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFRLDPEk 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  90 ---DVRPISGVVANLAVYSAFTNPGDVMIAPSIPAGGHISHG----KKEHSGTaglvhglDIEF--YPFDADEMT--IDV 158
Cdd:PLN03226 100 wgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtdGKKISAT-------SIYFesMPYRLDESTglIDY 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 159 DktkaKVEElKAANRLPKMAMFGGSLF--LFPHP-VKELSDFLKGYnihINYDAAHVAGLIAGGQFQDPLrEGADTMTMS 235
Cdd:PLN03226 173 D----KLEK-KAMLFRPKLIIAGASAYprDWDYArMRKIADKVGAL---LMCDMAHISGLVAAQEAASPF-EYCDVVTTT 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 236 THKTLFGPQGGLVLGREEHAEPIKK--------------ATFPGLTSSHHIHHMAAKAI--AFAEALEFgKQYAKDVIKN 299
Cdd:PLN03226 244 THKSLRGPRGGMIFFRKGPKPPKGQgegavydyedkinfAVFPGLQGGPHNHTIAALAValKQAMTPEF-KAYQKQVKAN 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 300 AKALADALSDAGFKVLGekrGYTKSHQIAVNVLDYS-DGGKVEADLEKANIIVNRQLIPGDIKAgrnyFHPGGIRLGVSE 378
Cdd:PLN03226 323 AAALANRLMSKGYKLVT---GGTDNHLVLWDLRPLGlTGSRVEKVLDLAHITLNKNAVPGDSSA----LVPGGVRIGTPA 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 851341915 379 LTRLGMKSAEMKEIAGYIKNIV-----IEKKDPKKLaakvKSFRK 418
Cdd:PLN03226 396 MTSRGLVEKDFEKVAEFLHRAVtialkIQKEHGKKL----KDFKK 436
PRK13580 PRK13580
glycine hydroxymethyltransferase;
27-399 3.22e-55

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 190.64  E-value: 3.22e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  27 SIPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKKLYKAKFADVRPISGVVANLAVYSA 106
Cdd:PRK13580  51 SLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAYVQPHSGADANLVAFWA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 107 ---------------FTNPGD----------------VMIAPSIPAGGHISHGKKEHsgtaglVHGLDIEFYPFDADEMT 155
Cdd:PRK13580 131 ilahkvespaleklgAKTVNDlteedwealraelgnqRLLGMSLDSGGHLTHGFRPN------ISGKMFHQRSYGVDPDT 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 156 --IDVDKTKAKVEELKaanrlPKMAMFGGSlfLFPHPV-----KELSDFLkGYNIHInyDAAHVAGLIAGGQFQ---DPL 225
Cdd:PRK13580 205 glLDYDEIAALAREFK-----PLILVAGYS--AYPRRVnfaklREIADEV-GAVLMV--DMAHFAGLVAGKVFTgdeDPV 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 226 REgADTMTMSTHKTLFGPQGGLVLGREEHAEPIKKATfPGLTSSHHIHHMAAKAIAFAEAL--EFgKQYAKDVIKNAKAL 303
Cdd:PRK13580 275 PH-ADIVTTTTHKTLRGPRGGLVLAKKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARtpEF-QKYAQQVVDNARAL 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 304 ADALSDAGFKVLgekRGYTKSHQIAVNVLDYSDGGKV-EADLEKANIIVNRQLIPGDiKAGRNYfhPGGIRLGVSELTRL 382
Cdd:PRK13580 352 AEGFLKRGARLV---TGGTDNHLVLIDVTSFGLTGRQaESALLDAGIVTNRNSIPSD-PNGAWY--TSGIRLGTPALTTL 425
                        410
                 ....*....|....*..
gi 851341915 383 GMKSAEMKEIAGYIKNI 399
Cdd:PRK13580 426 GMGSDEMDEVAELIVKV 442
PLN02271 PLN02271
serine hydroxymethyltransferase
28-396 6.25e-37

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 142.25  E-value: 6.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  28 IPLIASENVPSPAVKEALLSDFGNRYAEGWPGERVYAGCVYIDKVEIECMNLAKK---LYKAKFA-DVRPISGVVANLAV 103
Cdd:PLN02271 151 IELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAafgLDSEKWGvNVQPYSCTSANFAV 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 104 YSAFTNPGDVMIAPSIPAGGHISHGKKEHSGTAglVHGLDIEF--YPFDADEMT--IDVDktkaKVEElKAANRLPKMAM 179
Cdd:PLN02271 231 YTGLLLPGDRIMGLDSPSGGHMSHGYYTPGGKK--VSGASIFFesLPYKVNPQTgyIDYD----KLEE-KALDFRPKILI 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 180 FGGSlflfPHPvKELsDFLKGYNIH------INYDAAHVAGLIAGGQFQDPLrEGADTMTMSTHKTLFGPQGGLVLGRE- 252
Cdd:PLN02271 304 CGGS----SYP-REW-DYARFRQIAdkcgavLMCDMAHISGLVAAKECVNPF-DYCDIVTSTTHKSLRGPRGGIIFYRKg 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 253 -------------------EHAEPIKKATFPGLTSSHHIHHMAAKAIAFAEAL--EFgKQYAKDVIKNAKALADALSDAG 311
Cdd:PLN02271 377 pklrkqgmllshgddnshyDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVAtpEY-KAYMQQVKKNAQALASALLRRK 455
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 312 FKVLgekRGYTKSHQIAVNVLDYSDGGKV-EADLEKANIIVNRQLIPGDIKAgrnyFHPGGIRLGVSELTRLGMKSAEMK 390
Cdd:PLN02271 456 CRLV---TGGTDNHLLLWDLTTLGLTGKNyEKVCEMCHITLNKTAIFGDNGT----ISPGGVRIGTPAMTSRGCLESDFE 528

                 ....*.
gi 851341915 391 EIAGYI 396
Cdd:PLN02271 529 TIADFL 534
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
75-251 8.82e-14

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: 68.95  E-value: 8.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  75 ECMNLAKKLYKAKFADVRPI-SGVVANLAVYSAFTNPGDVMIapsIPAGGHISHgkkehSGTAGLVHGLDIEFYPFD-AD 152
Cdd:cd01494    4 ELEEKLARLLQPGNDKAVFVpSGTGANEAALLALLGPGDEVI---VDANGHGSR-----YWVAAELAGAKPVPVPVDdAG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 153 EMTIDVdktkAKVEELKAANRlPKMAMF--GGSLFLFPHPVKELSDFLKGYNIHINYDAAHvAGLIAGGQFQDPLREGAD 230
Cdd:cd01494   76 YGGLDV----AILEELKAKPN-VALIVItpNTTSGGVLVPLKEIRKIAKEYGILLLVDAAS-AGGASPAPGVLIPEGGAD 149
                        170       180
                 ....*....|....*....|.
gi 851341915 231 TMTMSTHKTLFGPQGGLVLGR 251
Cdd:cd01494  150 VVTFSLHKNLGGEGGGVVIVK 170
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
37-396 5.34e-07

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 51.15  E-value: 5.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915   37 PSPAVKEAL--LSDFGNRyaegwpgeRVYAGCVYIDKVEIEcmnLAKKLYKAKFADVRPISGVV-------ANLAVYSAF 107
Cdd:pfam00155  15 TLPAVAKAEkdALAGGTR--------NLYGPTDGHPELREA---LAKFLGRSPVLKLDREAAVVfgsgagaNIEALIFLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  108 TNPGDVMIapsIPAGGHISHGKkehsgtagLVHGLDIEFYPF---DADEMTIDVDKTKAKVEELkaanrlPKMaMFGGSL 184
Cdd:pfam00155  84 ANPGDAIL---VPAPTYASYIR--------IARLAGGEVVRYplyDSNDFHLDFDALEAALKEK------PKV-VLHTSP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  185 F-----LFPHP-VKELSDFLKGYNIHINYDAAHVAGLIAGGQFQDP---LREGADTMTMSTHKTLFGPQG---GLVLGRE 252
Cdd:pfam00155 146 HnptgtVATLEeLEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATralLAEGPNLLVVGSFSKAFGLAGwrvGYILGNA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  253 EHAEPIKKATFPGLTSSHHIHHMAAKAIAFAEALEFGKQYAKDVIKNAKALADALSDAGFKVLGEKRGYtkshqIAVNVL 332
Cdd:pfam00155 226 AVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGF-----FLLTGL 300
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 851341915  333 D-YSDGGKVEADLEKANIIVnrqlIPGdikagrNYFH-PGGIRLGVSeltrlGMKSAEMKEIAGYI 396
Cdd:pfam00155 301 DpETAKELAQVLLEEVGVYV----TPG------SSPGvPGWLRITVA-----GGTEEELEELLEAI 351
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
152-317 2.27e-06

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 439846 [Multi-domain]  Cd Length: 460  Bit Score: 49.83  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 152 DEMTIDVDKTKAKVEELKAANRLPkMAMFG--GSlflFPH----PVKELSDFLKGYNIHINYDAAHVAGLIAGGQFQDPL 225
Cdd:COG0076  198 EDGRMDPDALEAAIDEDRAAGLNP-IAVVAtaGT---TNTgaidPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLL 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 226 R--EGADTMTMSTHKTLFGPQG-GLVLGREEHAepikkatfpgLTSSHHIH------HMAAKAIAFAEALEFG------K 290
Cdd:COG0076  274 DgiERADSITVDPHKWLYVPYGcGAVLVRDPEL----------LREAFSFHasylgpADDGVPNLGDYTLELSrrfralK 343
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 851341915 291 QYA--------------KDVIKNAKALADALS-DAGFKVLGE 317
Cdd:COG0076  344 LWAtlralgregyreliERCIDLARYLAEGIAaLPGFELLAP 385
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
148-245 2.40e-05

DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.


Pssm-ID: 99743 [Multi-domain]  Cd Length: 345  Bit Score: 46.04  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 148 PFDADeMTIDVDKTKAKVEELKAANRLPkmAMFGGSLFLFPH----PVKELSDFLKGYNIHINYDAAHVAGLIAggqFQD 223
Cdd:cd06450  123 PVDED-GRMDPEALEAAIDEDKAEGLNP--IMVVATAGTTDTgaidPLEEIADLAEKYDLWLHVDAAYGGFLLP---FPE 196
                         90       100
                 ....*....|....*....|....*..
gi 851341915 224 PLR-----EGADTMTMSTHKTLFGPQG 245
Cdd:cd06450  197 PRHldfgiERVDSISVDPHKYGLVPLG 223
SelA pfam03841
L-seryl-tRNA selenium transferase;
190-260 2.80e-04

L-seryl-tRNA selenium transferase;


Pssm-ID: 309101  Cd Length: 367  Bit Score: 42.71  E-value: 2.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 851341915  190 PVKELSDFLKGYNIHINYDAAHVA-------GLIAGGQFQDPLREGADTMTMSTHKTLFGPQGGLVLGREEHAEPIKK 260
Cdd:pfam03841 158 ELAELVELGHEKGLPVYEDLGSGSlvdlsqyGLPKEPTVQELIAQGVDLVSFSGDKLLGGPQAGIIVGKKELIERIKK 235
SelA COG1921
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];
190-260 1.32e-03

Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441524  Cd Length: 399  Bit Score: 40.87  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915 190 PVKELSDFLKGYNIHINYDAAhvAG-LIAGGQF--------QDPLREGADTMTMSTHKTLFGPQGGLVLGREEHAEPIKK 260
Cdd:COG1921  176 SLAELAELAHEHGLPVIVDLG--SGsLVDLSKYglpheptvQEYLAAGADLVTFSGDKLLGGPQAGIIVGKKELIERIKK 253
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
95-325 2.16e-03

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 39.89  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915   95 SGVVANLAVYSAFTNPGDVMIApsipagGHISHGkkEHSGTAGLVHGLDIEFYPFDADEM-TIDVDKTKAKVEELKAANR 173
Cdd:pfam01212  55 SGTAANQLALMAHCQRGDEVIC------GEPAHI--HFDETGGHAELGGVQPRPLDGDEAgNMDLEDLEAAIREVGADIF 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  174 lPKMAM---------FGGSlflfPHP---VKELSDFLKGYNIHINYDAAHVA-GLIAGGqfqDPLRE---GADTMTMSTH 237
Cdd:pfam01212 127 -PPTGLislenthnsAGGQ----VVSlenLREIAALAREHGIPVHLDGARFAnAAVALG---VIVKEitsYADSVTMCLS 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851341915  238 KTLFGPQGGLVLGREE-----------HAEPIKKATFP---GLTSshhihhmaakaiafaeaLEFGKQYAKDVIKNAKAL 303
Cdd:pfam01212 199 KGLGAPVGSVLAGSDDfiakairqrkyLGGGLRQAGVLaaaGLRA-----------------LEEGVARLARDHATARRL 261
                         250       260
                  ....*....|....*....|..
gi 851341915  304 ADALSDAGFKVlgEKRGYTKSH 325
Cdd:pfam01212 262 AEGLELLRLAI--PRRVYTNTH 281
 
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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