ACL_RS00240

Uniprot: A9NEA9
Description: serine hydroxymethyltransferase
EC number: 2.1.2.1
Annotation score: 3 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine. {ECO:0000255|HAMAP-Rule:MF_00051}.
Cofactor: COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00051};
Enzyme regulation:
Function [CC]: FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. {ECO:0000255|HAMAP-Rule:MF_00051}.
Pathway: PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000255|HAMAP-Rule:MF_00051}.; PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}.
Active site:
Binding site: BINDING 30 30 Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 50 50 Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 52 52 Substrate. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 59 59 Substrate. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 60 60 Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 94 94 Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 116 116 Substrate; via carbonyl oxygen. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 171 171 Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 199 199 Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 224 224 Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 231 231 Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 257 257 Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen. {ECO:0000255|HAMAP-Rule:MF_00051}.; BINDING 358 358 Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_00051}.
Calcium binding:
DNA binding:
Metal binding:
Nucleotide binding:
Site:
Gene names (primary): glyA
Gene names (synonym):
Mass: 45,324
Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051}.
Gene ontology (GO): cytoplasm [GO:0005737]; glycine hydroxymethyltransferase activity [GO:0004372]; pyridoxal phosphate binding [GO:0030170]; glycine biosynthetic process from serine [GO:0019264]; tetrahydrofolate interconversion [GO:0035999]
Gene ontology IDs: GO:0004372; GO:0005737; GO:0019264; GO:0030170; GO:0035999
Chain: CHAIN 1 409 Serine hydroxymethyltransferase. /FTId=PRO_0000369893.
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP-Rule:MF_00051}.
Protein families: SHMT family
Coiled coil:
Domain [FT]:
Motif:
Region: REGION 120 122 Substrate binding. {ECO:0000255|HAMAP-Rule:MF_00051}.
EMBL: CP000896
ProteinModelPortal: A9NEA9
MEROPS:
EnsemblBacteria KO: ABX80689
UniPathway: K00600
CDD:
Gene3D: cd00378
HAMAP: 3.40.640.10;3.90.1150.10
InterPro: MF_00051
PANTHER: IPR015424;IPR015421;IPR015422;IPR001085;IPR019798
PIRSF: PTHR11680
PRINTS: PIRSF000412
PROSITE:
Pfam: PS00096
ProDom: PF00464
SMART:
SUPFAM:
TIGRFAMs: SSF53383

57169-58399(+)

>nucleotide sequence
ATGACATTAAAAGACTATGATCTTGAATTATTTAACGCGATTCAAAGAGAAGATAACAGA
CAAAAAGAACACATCGAATTAATTGCGTCCGAAAACTTTGTTTCTGATGCAGTGTTAGAG
GCACAAGGTTCAATTTTAACCAACAAATATGCAGAAGGCTATCCAAATAAAAGATATTAT
GGAGGTTGCGAATTTGTTGATCAAGTAGAGATACTAGCTCAAGATAGGTTAAAACAAATC
TTTAATGCGAAGTTTGTAAATGTACAGCCTCATTCGGGTTCACAGGCTAATGCTGCTGTT
TATCAGGCACTACTTAGTCCCGGAGACAGGGTTTTAGGAATGGATTTAAATGCGGGTGGT
CACTTAACTCATGGTTATAAATTATCATTTTCTGGACATTATTATGAAGCACATGCCTAT
GGTGTAAGTAGGTTTGATGAAAGAATTGATTATGAAGAAGTACTGAAAATTGCAATTGAA
GTTAAACCTAAAATGATTATTGCAGGTGCGAGTGCATATCCAAGAGTCATTGATTTTAAA
AAGTTTAGAGAAATTGCAGATACAGTTGGTGCATACTTGTTTGTAGATATGGCACATATT
GCAGGACTAGTTGCTTGTGGATTACATCCATCACCACTACCTTATGCAGATGTTGTCACG
TCTACTACACATAAAACCTTAAGAGGTCCACGTGGTGGTATTATACTTACAAATGATGCA
AGTATTGCTAAAAAAATAGATCGTGCAGTATTTCCTGGCCAACAAGGTGGTCCATTAATG
CACATTATTGCTGCAAAGGCGGTTGCATTTAAAGAAGCACTAGACCCTAACTTTAAGGTA
TATCAAACACAAGTGATTAAAAATGCTAAAGCCTTAAGTGATACATTCAAATCACTTGGA
TATAAATTAATTTCAGATGGTACAGATAATCATTTAATCTTAGTAGATGTTAAATCAAAA
TTAGGTATTACAGGAAGAGATGCTGAGGATGCGCTATATAAAGCAAATATCACAATCAAT
AAAAACCAGTTACCGTTTGATCAAGAAAAACCGATGTTAACCTCAGGTATAAGATTAGGA
ACACCTGCGATGACAACTAAGGGTTTTAAAGAAAATGAGTTTATTAAAGTAGCACAACTT
ATTGATGAAGTGTTATCGAATATAAACAATGAAGAAGTTATCAATAAAGTTAAAAAAGAA
GTACTAAAACTAATGAAAGATGTTAAATGA

>protein sequence
MTLKDYDLELFNAIQREDNRQKEHIELIASENFVSDAVLEAQGSILTNKYAEGYPNKRYY
GGCEFVDQVEILAQDRLKQIFNAKFVNVQPHSGSQANAAVYQALLSPGDRVLGMDLNAGG
HLTHGYKLSFSGHYYEAHAYGVSRFDERIDYEEVLKIAIEVKPKMIIAGASAYPRVIDFK
KFREIADTVGAYLFVDMAHIAGLVACGLHPSPLPYADVVTSTTHKTLRGPRGGIILTNDA
SIAKKIDRAVFPGQQGGPLMHIIAAKAVAFKEALDPNFKVYQTQVIKNAKALSDTFKSLG
YKLISDGTDNHLILVDVKSKLGITGRDAEDALYKANITINKNQLPFDQEKPMLTSGIRLG
TPAMTTKGFKENEFIKVAQLIDEVLSNINNEEVINKVKKEVLKLMKDVKW