ID GLYA_BACV8 Reviewed; 426 AA.
AC A6L5K3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 01-MAY-2013, entry version 48.
DE RecName: Full=Serine hydroxymethyltransferase;
DE Short=SHMT;
DE Short=Serine methylase;
DE EC=2.1.2.1;
GN Name=glyA; OrderedLocusNames=BVU_3341;
OS Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=435590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8482 / DSM 1447 / NCTC 11154;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M.,
RA Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P.,
RA Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A.,
RA Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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; CP000139; ABR40967.1; -; Genomic_DNA.
DR RefSeq; YP_001300589.1; NC_009614.1.
DR ProteinModelPortal; A6L5K3; -.
DR SMR; A6L5K3; 2-418.
DR STRING; 435590.BVU_3341; -.
DR EnsemblBacteria; ABR40967; ABR40967; BVU_3341.
DR GeneID; 5304302; -.
DR KEGG; bvu:BVU_3341; -.
DR PATRIC; 21071710; VBIBacVul85104_3436.
DR eggNOG; COG0112; -.
DR HOGENOM; HOG000239403; -.
DR KO; K00600; -.
DR OMA; IAKLQWA; -.
DR ProtClustDB; PRK00011; -.
DR BioCyc; BVUL435590:GH96-3353-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 1 426 Serine hydroxymethyltransferase.
FT /FTId=PRO_1000006222.
FT REGION 117 119 Substrate binding (By similarity).
FT REGION 363 365 Substrate binding (By similarity).
FT BINDING 27 27 Pyridoxal phosphate (By similarity).
FT BINDING 47 47 Pyridoxal phosphate (By similarity).
FT BINDING 49 49 Substrate (By similarity).
FT BINDING 56 56 Substrate (By similarity).
FT BINDING 57 57 Pyridoxal phosphate (By similarity).
FT BINDING 113 113 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 168 168 Pyridoxal phosphate (By similarity).
FT BINDING 196 196 Pyridoxal phosphate (By similarity).
FT BINDING 221 221 Pyridoxal phosphate (By similarity).
FT BINDING 228 228 Pyridoxal phosphate (By similarity).
FT BINDING 269 269 Pyridoxal phosphate; via amide nitrogen
FT and carbonyl oxygen (By similarity).
FT BINDING 371 371 Pyridoxal phosphate (By similarity).
FT MOD_RES 222 222 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 426 AA; 46827 MW; 007F3EF0206192ED CRC64;
MKRDDLIFDI IEKEHQRQLK GIELIASENF VSDQVMQAMG SCLTNKYAEG YPGKRYYGGC
EVVDQSEQIA IDRLKQIFGA EWANVQPHSG AQANAAVFLA VLNPGDKFMG LNLAHGGHLS
HGSLVNTSGI IYTPCEYNLN KETGRVDYDQ MEEIALREKP KMIIGGGSAY SREWDYKRMR
EIADKVGAIL MIDMAHPAGL IAAGLLDNPV KYAHIVTSTT HKTLRGPRGG VIMMGKDFPN
PWGKKTPKGE IKMMSQLLDS AVFPGIQGGP LEHVIAAKAV AFGECLQPEY KEYQTQVKKN
AAVLAQALID RGFTIVSGGT DNHSMLVDLR TKYPDLTGKV AEKALVAADI TVNKNMVPFD
SRSAFQTSGI RLGTPAITTR GAKEDLMLEI AEMIETVLSN VDNEEVIAQV RARVNETMKK
YPIFAY
//
