ID GLYA_ACIB5 Reviewed; 417 AA.
AC B7I2R7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 34.
DE RecName: Full=Serine hydroxymethyltransferase;
DE Short=SHMT;
DE Short=Serine methylase;
DE EC=2.1.2.1;
GN Name=glyA; OrderedLocusNames=AB57_2665;
OS Acinetobacter baumannii (strain AB0057).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Moraxellaceae; Acinetobacter;
OC Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=480119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB0057;
RX PubMed=18931120; DOI=10.1128/JB.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H.,
RA Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A.,
RA Hujer A.M., Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant
RT Acinetobacter baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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 (By similarity).
CC -!- SIMILARITY: Belongs to the SHMT family.
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DR EMBL; CP001182; ACJ42769.1; -; Genomic_DNA.
DR RefSeq; YP_002320005.1; NC_011586.1.
DR ProteinModelPortal; B7I2R7; -.
DR SMR; B7I2R7; 5-416.
DR STRING; 480119.AB57_2665; -.
DR EnsemblBacteria; ACJ42769; ACJ42769; AB57_2665.
DR GeneID; 7044278; -.
DR KEGG; abn:AB57_2665; -.
DR PATRIC; 20699039; VBIAciBau111166_2575.
DR eggNOG; COG0112; -.
DR HOGENOM; HOG000239404; -.
DR KO; K00600; -.
DR OMA; IAKLQWA; -.
DR ProtClustDB; PRK00011; -.
DR BioCyc; ABAU480119:GHQY-3365-MONOMER; -.
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; Complete proteome; Cytoplasm;
KW One-carbon metabolism; Pyridoxal phosphate; Transferase.
FT CHAIN 1 417 Serine hydroxymethyltransferase.
FT /FTId=PRO_1000116817.
FT REGION 124 126 Substrate binding (By similarity).
FT REGION 354 356 Substrate binding (By similarity).
FT BINDING 34 34 Pyridoxal phosphate (By similarity).
FT BINDING 54 54 Pyridoxal phosphate (By similarity).
FT BINDING 56 56 Substrate (By similarity).
FT BINDING 63 63 Substrate (By similarity).
FT BINDING 64 64 Pyridoxal phosphate (By similarity).
FT BINDING 98 98 Pyridoxal phosphate (By similarity).
FT BINDING 120 120 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 262 262 Pyridoxal phosphate; via amide nitrogen
FT and carbonyl oxygen (By similarity).
FT BINDING 362 362 Pyridoxal phosphate (By similarity).
FT MOD_RES 229 229 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 417 AA; 44995 MW; C6D7ACE5AEFF75B8 CRC64;
MFANISISEF DPELAQAIAS EDERQEAHIE LIASENYCSP AVMEAQGSKL TNKYAEGYPG
KRYYGGCEFV DVIEQMAIDR AKELFGADYA NVQPHAGSQA NSAVYLALLN PGDTVLGMSL
AHGGHLTHGA KVSFSGKTYN AVQYGLNAET GEIDYEEVER LALEHKPRMI VAGFSAYSRV
VDWQRFRDIA DKVGAYLFVD MAHVAGLVAA GVYPNPVQIA DVTTTTTHKT LRGPRSGLIL
AKANEEIEKK LQSAVFPGNQ GGPLMHAIAA KAICFKEAMS DDFKAYQQQV VKNAQAMAEV
FIARGYDVVS GGTDNHLFLL SLIKQDVTGK DADAWLGAAH ITVNKNSVPN DPRSPFVTSG
IRIGTPAVTT RGFGEAEVRE LAGWIADVID SKGDEKVIAD VKAKVEAVCA KFPVYAK
//
