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Database: UniProt
Entry: A6L5K3
LinkDB: A6L5K3
Original site: A6L5K3 
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   19-FEB-2014, entry version 52.
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; MLIDLRN; -.
DR   OrthoDB; EOG6Z0QB2; -.
DR   ProtClustDB; PRK00011; -.
DR   BioCyc; BVUL435590:GH96-3333-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: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; 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
//
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