GenomeNet

Database: UniProt
Entry: A6TQQ1
LinkDB: A6TQQ1
Original site: A6TQQ1 
ID   GLYA_ALKMQ              Reviewed;         410 AA.
AC   A6TQQ1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   14-MAY-2014, entry version 49.
DE   RecName: Full=Serine hydroxymethyltransferase;
DE            Short=SHMT;
DE            Short=Serine methylase;
DE            EC=2.1.2.1;
GN   Name=glyA; OrderedLocusNames=Amet_2365;
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Ye Q.,
RA   Zhou J., Fields M., Richardson P.;
RT   "Complete sequence of Alkaliphilus metalliredigens QYMF.";
RL   Submitted (JUN-2007) 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000724; ABR48519.1; -; Genomic_DNA.
DR   RefSeq; YP_001320178.1; NC_009633.1.
DR   ProteinModelPortal; A6TQQ1; -.
DR   SMR; A6TQQ1; 6-404.
DR   STRING; 293826.Amet_2365; -.
DR   EnsemblBacteria; ABR48519; ABR48519; Amet_2365.
DR   GeneID; 5312437; -.
DR   KEGG; amt:Amet_2365; -.
DR   eggNOG; COG0112; -.
DR   HOGENOM; HOG000239403; -.
DR   KO; K00600; -.
DR   OMA; ANMIELE; -.
DR   OrthoDB; EOG6Z0QB2; -.
DR   BioCyc; AMET293826:GI5P-2410-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    410       Serine hydroxymethyltransferase.
FT                                /FTId=PRO_1000057362.
FT   REGION      123    125       Substrate binding (By similarity).
FT   REGION      351    353       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     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     259    259       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen (By similarity).
FT   BINDING     359    359       Pyridoxal phosphate (By similarity).
FT   MOD_RES     228    228       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   410 AA;  45223 MW;  55F9893A45D63B94 CRC64;
     MNFDTLKKFD EEIYEVIQKE TKRQRGSIEL IASENFVTTA VMEAMGSQLT NKYAEGYPDK
     RYYGGCEEVD VAENLARNRL KKLFNAEHAN VQPHSGANAN IGVYFATLEP GDTVLGMNLS
     HGGHLTHGSP VNISGAYYNF VAYGVDSVTH RIDYEEVMRV AQEAKPKMIV AGASAYPRAI
     DFKKFREIAD AVGAYLMVDM AHIAGLVAVG LHQNPCEYAD FVTTTTHKTL RGPRGGAILC
     KEKYAKIIDK AIFPGLQGGP LMHVIAAKAV AFKEALEPGF KAYQEQVIKN AKALGEELKK
     QGFDLVSDGT DTHLLLIDLR NKNITGKDAE RLFDEVGITV NKNTIPFDPQ SPFVTSGIRI
     GTPAVTTRGM KEEEMKKIAG VMNIIIDHPE KVSEAQKVVD ELCNQFKLYE
//
DBGET integrated database retrieval system