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Conserved domains on  [gi|1696246688|ref|WP_141123983|]
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serine hydroxymethyltransferase, partial [Pseudomonas borbori]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 1-229 1.01e-160

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).


The actual alignment was detected with superfamily member PRK00011:

Pssm-ID: 450240  Cd Length: 416  Bit Score: 450.68  E-value: 1.01e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAKaNPEIEKKLNAAVFPGAQGGPLMH 80
Cdd:PRK00011  186 REIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTN-DEELAKKINSAVFPGIQGGPLMH 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  81 VIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAGITVNKN 160
Cdd:PRK00011  265 VIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKN 344

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696246688 161 SVPNDPQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWICDILDHLGDADVEARVAELAAGLCADYPVY 229
Cdd:PRK00011  345 AVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEEVKELCKRFPLY 413
 
Name Accession Description Interval E-value
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
 1-229 1.01e-160

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 450.68  E-value: 1.01e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAKaNPEIEKKLNAAVFPGAQGGPLMH 80
Cdd:PRK00011  186 REIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTN-DEELAKKINSAVFPGIQGGPLMH 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  81 VIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAGITVNKN 160
Cdd:PRK00011  265 VIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKN 344

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696246688 161 SVPNDPQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWICDILDHLGDADVEARVAELAAGLCADYPVY 229
Cdd:PRK00011  345 AVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEEVKELCKRFPLY 413
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
 1-229 8.02e-158

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: 443.32  E-value: 8.02e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAkaNPEIEKKLNAAVFPGAQGGPLMH 80
Cdd:COG0112   185 REIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILC--NEELAKKIDSAVFPGLQGGPLMH 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  81 VIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAGITVNKN 160
Cdd:COG0112   263 VIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKN 342

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696246688 161 SVPNDPQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWICDILDHLGDADVEARVAELAAGLCADYPVY 229
Cdd:COG0112   343 AIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEVKELCKRFPLY 411
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
 1-218 4.09e-120

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: 347.27  E-value: 4.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAKaNPEIEKKLNAAVFPGAQGGPLMH 80
Cdd:cd00378   182 REIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTR-KGELAKKINSAVFPGLQGGPHLH 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  81 VIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAGITVNKN 160
Cdd:cd00378   261 VIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKN 340

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696246688 161 SVPNDPQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWICDIL-DHLGDADVEA---RVAEL 218
Cdd:cd00378   341 TLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALkDAEDVAVAEEvrkEVAEL 402
SHMT pfam00464
Serine hydroxymethyltransferase;
1-199 4.38e-113

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 329.40  E-value: 4.38e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAKANP------------EIEKKLNAA 68
Cdd:pfam00464 190 REIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIFYRKGVksvdktgkeilyELEKKINSA 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  69 VFPGAQGGPLMHVIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADA 148
Cdd:pfam00464 270 VFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERGYKLVSGGTDNHLVLVDLRPKGLDGARAEK 349

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1696246688 149 ALGRAGITVNKNSVPNDpQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWI 199
Cdd:pfam00464 350 VLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
 
Name Accession Description Interval E-value
glyA PRK00011
serine hydroxymethyltransferase; Reviewed
 1-229 1.01e-160

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 234571  Cd Length: 416  Bit Score: 450.68  E-value: 1.01e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAKaNPEIEKKLNAAVFPGAQGGPLMH 80
Cdd:PRK00011  186 REIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTN-DEELAKKINSAVFPGIQGGPLMH 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  81 VIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAGITVNKN 160
Cdd:PRK00011  265 VIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKN 344

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696246688 161 SVPNDPQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWICDILDHLGDADVEARVAELAAGLCADYPVY 229
Cdd:PRK00011  345 AVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEEVKELCKRFPLY 413
GlyA COG0112
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ...
 1-229 8.02e-158

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: 443.32  E-value: 8.02e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAkaNPEIEKKLNAAVFPGAQGGPLMH 80
Cdd:COG0112   185 REIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILC--NEELAKKIDSAVFPGLQGGPLMH 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  81 VIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAGITVNKN 160
Cdd:COG0112   263 VIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKN 342

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696246688 161 SVPNDPQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWICDILDHLGDADVEARVAELAAGLCADYPVY 229
Cdd:COG0112   343 AIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEVKELCKRFPLY 411
PRK13034 PRK13034
serine hydroxymethyltransferase; Reviewed
 1-229 6.13e-154

serine hydroxymethyltransferase; Reviewed


Pssm-ID: 237280  Cd Length: 416  Bit Score: 433.62  E-value: 6.13e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAKaNPEIEKKLNAAVFPGAQGGPLMH 80
Cdd:PRK13034  189 REIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTN-DEEIAKKINSAVFPGLQGGPLMH 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  81 VIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAGITVNKN 160
Cdd:PRK13034  268 VIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKN 347

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1696246688 161 SVPNDPQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWICDILDHLGDADVEARVAELAAGLCADYPVY 229
Cdd:PRK13034  348 TVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRKEVKALCSRFPIY 416
SHMT cd00378
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ...
 1-218 4.09e-120

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: 347.27  E-value: 4.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAKaNPEIEKKLNAAVFPGAQGGPLMH 80
Cdd:cd00378   182 REIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTR-KGELAKKINSAVFPGLQGGPHLH 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  81 VIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAGITVNKN 160
Cdd:cd00378   261 VIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKN 340

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696246688 161 SVPNDPQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWICDIL-DHLGDADVEA---RVAEL 218
Cdd:cd00378   341 TLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALkDAEDVAVAEEvrkEVAEL 402
SHMT pfam00464
Serine hydroxymethyltransferase;
1-199 4.38e-113

Serine hydroxymethyltransferase;


Pssm-ID: 395372  Cd Length: 399  Bit Score: 329.40  E-value: 4.38e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAKANP------------EIEKKLNAA 68
Cdd:pfam00464 190 REIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIFYRKGVksvdktgkeilyELEKKINSA 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  69 VFPGAQGGPLMHVIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADA 148
Cdd:pfam00464 270 VFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERGYKLVSGGTDNHLVLVDLRPKGLDGARAEK 349

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1696246688 149 ALGRAGITVNKNSVPNDpQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWI 199
Cdd:pfam00464 350 VLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
PTZ00094 PTZ00094
serine hydroxymethyltransferase; Provisional
 1-199 1.57e-94

serine hydroxymethyltransferase; Provisional


Pssm-ID: 240264  Cd Length: 452  Bit Score: 283.80  E-value: 1.57e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILA--KANPEIEKKLNAAVFPGAQGGPL 78
Cdd:PTZ00094  203 REICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSGLIFYrkKVKPDIENKINEAVFPGLQGGPH 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  79 MHVIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAGITVN 158
Cdd:PTZ00094  283 NHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVN 362

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1696246688 159 KNSVPNDpQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWI 199
Cdd:PTZ00094  363 KNTIPGD-KSALNPSGVRLGTPALTTRGAKEKDFKFVADFL 402
PRK13580 PRK13580
glycine hydroxymethyltransferase;
1-229 3.31e-91

glycine hydroxymethyltransferase;


Pssm-ID: 184161  Cd Length: 493  Bit Score: 276.54  E-value: 3.31e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYP---NPIPFADVVTTTTHKTLRGPRGGLILAKanPEIEKKLNAAVfPGAQGGP 77
Cdd:PRK13580  241 REIADEVGAVLMVDMAHFAGLVAGKVFTgdeDPVPHADIVTTTTHKTLRGPRGGLVLAK--KEYADAVDKGC-PLVLGGP 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  78 LMHVIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADAALGRAGITV 157
Cdd:PRK13580  318 LPHVMAAKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVT 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688 158 NKNSVPNDPQSPFVTSGLRIGTPAITTRGFKEQQSIELAGWICDILDHLG----------------DADVEARVAELAAG 221
Cdd:PRK13580  398 NRNSIPSDPNGAWYTSGIRLGTPALTTLGMGSDEMDEVAELIVKVLSNTTpgttaegapskakyelDEGVAQEVRARVAE 477


                  ....*...
gi 1696246688 222 LCADYPVY 229
Cdd:PRK13580  478 LLARFPLY 485
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
 1-189 7.86e-90

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 272.63  E-value: 7.86e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAKANP------------EIEKKLNAA 68
Cdd:PLN03226  204 RKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGGMIFFRKGPkppkgqgegavyDYEDKINFA 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  69 VFPGAQGGPLMHVIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLTGKDADA 148
Cdd:PLN03226  284 VFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEK 363

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1696246688 149 ALGRAGITVNKNSVPNDpQSPFVTSGLRIGTPAITTRGFKE 189
Cdd:PLN03226  364 VLDLAHITLNKNAVPGD-SSALVPGGVRIGTPAMTSRGLVE 403
PLN02271 PLN02271
serine hydroxymethyltransferase
 1-186 7.25e-56

serine hydroxymethyltransferase


Pssm-ID: 215153  Cd Length: 586  Bit Score: 187.32  E-value: 7.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAKANPEI------------------E 62
Cdd:PLN02271  319 RQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRGGIIFYRKGPKLrkqgmllshgddnshydfE 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  63 KKLNAAVFPGAQGGPLMHVIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVSGGTDNHLFLVSLIRQGLT 142
Cdd:PLN02271  399 EKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALASALLRRKCRLVTGGTDNHLLLWDLTTLGLT 478

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1696246688 143 GKDADAALGRAGITVNKNSV--PNDPQSPfvtSGLRIGTPAITTRG 186
Cdd:PLN02271  479 GKNYEKVCEMCHITLNKTAIfgDNGTISP---GGVRIGTPAMTSRG 521
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 1-56 9.97e-10

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: 55.85  E-value: 9.97e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1696246688   1 RAIADKVGALLFVDMAHVAGLVAAGLYPNPIPFADVVTTTTHKTLRGPRGGLILAK 56
Cdd:cd01494   115 RKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEGGGVVIVK 170
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
2-184 3.80e-05

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 43.83  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   2 AIADKVGALLFVDMAHVAGLVAAGLYPNPIPFAD-----VVTTTTHKT--LRGPRGGLILakANPEIEKKLNAAVFPGAQ 74
Cdd:pfam00155 163 DLAKEHNILLLVDEAYAGFVFGSPDAVATRALLAegpnlLVVGSFSKAfgLAGWRVGYIL--GNAAVISQLRKLARPFYS 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  75 GGPLMHvIAAKAVCFKEALEPGFKEYQAQVIKNAQAMAKVFIERGFDVVsgGTDNHLFLVSLIRQGLTGKDADAALGRAG 154
Cdd:pfam00155 241 STHLQA-AAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVL--PSQAGFFLLTGLDPETAKELAQVLLEEVG 317

                         170       180       190
                  ....*....|....*....|....*....|
gi 1696246688 155 ITVNKNSvpndpqSPFVTSGLRIGTPAITT 184
Cdd:pfam00155 318 VYVTPGS------SPGVPGWLRITVAGGTE 341
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 2-171 1.54e-03

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 38.86  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   2 AIADKVGALLFVDMAHvAGLVAAGLYPNPIPFAD-----VVTTTTHKTLRGP--RGGLILAKaNPEIEKKLNAAVFPGAQ 74
Cdd:cd00609   159 ELAKKHGILIISDEAY-AELVYDGEPPPALALLDayervIVLRSFSKTFGLPglRIGYLIAP-PEELLERLKKLLPYTTS 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688  75 GGPlmhVIAAKAVCfkEALEPG---FKEYQAQVIKNAQAMAKVFIERGFDVV---SGGtdNHLFLVslIRQGLTGKDADA 148
Cdd:cd00609   237 GPS---TLSQAAAA--AALDDGeehLEELRERYRRRRDALLEALKELGPLVVvkpSGG--FFLWLD--LPEGDDEEFLER 307

                         170       180
                  ....*....|....*....|...
gi 1696246688 149 ALGRAGITVNKNSVPNDPQSPFV 171
Cdd:cd00609   308 LLLEAGVVVRPGSAFGEGGEGFV 330
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 2-130 5.39e-03

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: 37.16  E-value: 5.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696246688   2 AIADKVGALLFVDMAHV--------AGLVAAGLYPNPIpfaDVVTTTTHKTLrGPRGGLILAKAnPEIEKKLNAA---VF 70
Cdd:cd06454   156 DLAKKYGAILFVDEAHSvgvygphgRGVEEFGGLTDDV---DIIMGTLGKAF-GAVGGYIAGSK-ELIDYLRSYArgfIF 230

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1696246688  71 PGAQggPLMHVIAAKAvcfkeALE--PGFKEYQAQVIKNAQAMAKVFIERGFDVvsGGTDNH 130
Cdd:cd06454   231 STSL--PPAVAAAALA-----ALEvlQGGPERRERLQENVRYLRRGLKELGFPV--GGSPSH 283
 
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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