ID GLYA_PELLD Reviewed; 440 AA.
AC Q3B2I7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 01-MAY-2013, entry version 57.
DE RecName: Full=Serine hydroxymethyltransferase;
DE Short=SHMT;
DE Short=Serine methylase;
DE EC=2.1.2.1;
GN Name=glyA; OrderedLocusNames=Plut_1590;
OS Pelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM
OS 273)).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=319225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 273;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelodictyon luteolum DSM 273.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000096; ABB24444.1; -; Genomic_DNA.
DR RefSeq; YP_375487.1; NC_007512.1.
DR ProteinModelPortal; Q3B2I7; -.
DR SMR; Q3B2I7; 4-428.
DR STRING; 319225.Plut_1590; -.
DR PRIDE; Q3B2I7; -.
DR EnsemblBacteria; ABB24444; ABB24444; Plut_1590.
DR GeneID; 3746116; -.
DR KEGG; plt:Plut_1590; -.
DR PATRIC; 21380822; VBIChlLut1287_1669.
DR eggNOG; COG0112; -.
DR HOGENOM; HOG000239405; -.
DR KO; K00600; -.
DR OMA; MMSEVID; -.
DR ProtClustDB; PRK00011; -.
DR BioCyc; PLUT319225:GHDM-1606-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 1 440 Serine hydroxymethyltransferase.
FT /FTId=PRO_0000234997.
FT REGION 123 125 Substrate binding (By similarity).
FT REGION 370 372 Substrate binding (By similarity).
FT BINDING 33 33 Pyridoxal phosphate (By similarity).
FT BINDING 53 53 Pyridoxal phosphate (By similarity).
FT BINDING 55 55 Substrate (By similarity).
FT BINDING 62 62 Substrate (By similarity).
FT BINDING 63 63 Pyridoxal phosphate (By similarity).
FT BINDING 97 97 Pyridoxal phosphate (By similarity).
FT BINDING 119 119 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 174 174 Pyridoxal phosphate (By similarity).
FT BINDING 202 202 Pyridoxal phosphate (By similarity).
FT BINDING 227 227 Pyridoxal phosphate (By similarity).
FT BINDING 234 234 Pyridoxal phosphate (By similarity).
FT BINDING 278 278 Pyridoxal phosphate; via amide nitrogen
FT and carbonyl oxygen (By similarity).
FT BINDING 378 378 Pyridoxal phosphate (By similarity).
FT MOD_RES 228 228 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 440 AA; 47799 MW; 2CA44417FC89D757 CRC64;
MDTDILKMQD REVFDAIAGE TVRQMETLEL IASENFTSRA VMQACGSVMT NKYAEGYPGK
RYYGGCEFVD IAEDLARERA RKLFGCEYVN VQPHSGSSAN MAVLFSVLKP GDRIMGLDLS
HGGHLTHGSS VNFSGQMFDA RSYGVDRETG IIDMNKVEEM ALDFKPRLII CGASAYSQGF
DFKAFREIAD KVGAFLMADI AHPAGLIAAG LLTDPMPHCH FVTTTTHKTL RGPRGGMIMM
GKDFENPMGI TIKTKNGPRV KMMSEVMDAE VMPGIQGGPL MHIIAGKAVA FGEALRPEFR
EYAVQVRKNA ASMAERFTSL GYNIVSGGTK NHLMLLDLRN KDVNGKVAEN LLHDAGITVN
KNMVPFDDKS PFVTSGIRIG TAAMTTRGMK EADATLIAEL IDRVITGAAE STIAATCKDV
KAEIRSLCLQ NPLEGYGVTP
//
