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 03-APR-2013, entry version 80.
DE RecName: Full=Serine hydroxymethyltransferase;
DE Short=SHMT;
DE Short=Serine methylase;
DE EC=2.1.2.1;
GN Name=glyA;
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 (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
CC H(2)O = tetrahydrofolate + L-serine.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC from L-serine: step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the SHMT family.
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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-SubCell.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA: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; PyrdxlP-dep_Trfase_major; 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 (By similarity).
FT BINDING 35 35 Pyridoxal phosphate (By similarity).
FT BINDING 55 55 Pyridoxal phosphate (By similarity).
FT BINDING 57 57 Substrate (By similarity).
FT BINDING 64 64 Substrate (By similarity).
FT BINDING 65 65 Pyridoxal phosphate (By similarity).
FT BINDING 99 99 Pyridoxal phosphate (By similarity).
FT BINDING 121 121 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 175 175 Pyridoxal phosphate (By similarity).
FT BINDING 203 203 Pyridoxal phosphate (By similarity).
FT BINDING 228 228 Pyridoxal phosphate (By similarity).
FT BINDING 235 235 Pyridoxal phosphate (By similarity).
FT BINDING 263 263 Pyridoxal phosphate; via amide nitrogen
FT and carbonyl oxygen (By similarity).
FT BINDING 363 363 Pyridoxal phosphate (By similarity).
FT MOD_RES 229 229 N6-(pyridoxal phosphate)lysine (By
FT similarity).
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
//
