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Database: UniProt
Entry: P34894
LinkDB: P34894
Original site: P34894 
ID   GLYA_AGGAC              Reviewed;         420 AA.
AC   P34894;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   26-NOV-2014, entry version 85.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051};
DE            EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051};
OS   Aggregatibacter actinomycetemcomitans (Actinobacillus
OS   actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8300209;
RA   Brogan J.M., Lally E.T., Poulsen K., Kilian M., Demuth D.R.;
RT   "Regulation of Actinobacillus actinomycetemcomitans leukotoxin
RT   expression: analysis of the promoter regions of leukotoxic and
RT   minimally leukotoxic strains.";
RL   Infect. Immun. 62:501-508(1994).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with tetrahydrofolate (THF) serving as the one-carbon
CC       carrier. This reaction serves as the major source of one-carbon
CC       groups required for the biosynthesis of purines, thymidylate,
CC       methionine, and other important biomolecules. Also exhibits THF-
CC       independent aldolase activity toward beta-hydroxyamino acids,
CC       producing glycine and aldehydes, via a retro-aldol mechanism.
CC       {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
CC       H(2)O = tetrahydrofolate + L-serine. {ECO:0000255|HAMAP-
CC       Rule:MF_00051}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00051};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC       from L-serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00051}.
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DR   EMBL; Z23269; CAA80807.1; -; Genomic_DNA.
DR   PIR; S34379; S34379.
DR   ProteinModelPortal; P34894; -.
DR   SMR; P34894; 1-420.
DR   PRIDE; P34894; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-HAMAP.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00051; SHMT; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR   PANTHER; PTHR11680; PTHR11680; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00096; SHMT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; One-carbon metabolism;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN         1    420       Serine hydroxymethyltransferase.
FT                                /FTId=PRO_0000113518.
FT   REGION      125    127       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      35     35       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      55     55       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      57     57       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      64     64       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      65     65       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      99     99       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     121    121       Substrate; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00051}.
FT   BINDING     175    175       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     203    203       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     228    228       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     235    235       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     263    263       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     363    363       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   MOD_RES     229    229       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00051}.
SQ   SEQUENCE   420 AA;  45790 MW;  62AE04DA1AF0062E CRC64;
     MFKKSMNIAD YDPVLWQAIE NENRRQEEHI ELIASENYAS PRVMQAQGSQ FTNKYAEGYP
     GKRYYGGCEY ADIVEQLAIE RAKELFGADY VNVQPHSGSQ ANAAVYMGLL NPGDTILGMS
     LAHGGHLTHG ASVSFSGKIY HAEQYGITDE GLIDYDALRK QAHDVKPKMI VGGFSAYSQV
     VDWKKMREIA DEVGAYLFVD MAHVAGLVAA GIYPNPLPYA HVVTTTTHKT LGGPRGGLIL
     SSCGDEEIYK KLNSAVFPAG QGGPLVHIIA AKAVCFKEAL EPEYKVYQQN VLKNAKAMVE
     VFKQRCYKVV SNGTENHLFL VDLVSHGLTG KAADAALGKA NITVNKNSVP NDPQKPFITS
     GIRVGTPSVT RRGFNEADVK ELAGWMCDVL DAIGKDNEAE VIADTKDKVL AICKRLPVYA
//
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