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Database: UniProt
Entry: Q6L1F6
LinkDB: Q6L1F6
Original site: Q6L1F6 
ID   GLYA_PICTO              Reviewed;         433 AA.
AC   Q6L1F6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-SEP-2014, entry version 75.
DE   RecName: Full=Serine hydroxymethyltransferase;
DE            Short=SHMT;
DE            Short=Serine methylase;
DE            EC=2.1.2.-;
GN   Name=glyA; OrderedLocusNames=PTO0611;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with a modified folate serving as the one-carbon carrier.
CC       Also exhibits a pteridine-independent aldolase activity toward
CC       beta-hydroxyamino acids, producing glycine and aldehydes, via a
CC       retro-aldol mechanism (By similarity).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
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; AE017261; AAT43196.1; -; Genomic_DNA.
DR   RefSeq; WP_011177412.1; NC_005877.1.
DR   RefSeq; YP_023389.1; NC_005877.1.
DR   ProteinModelPortal; Q6L1F6; -.
DR   STRING; 263820.PTO0611; -.
DR   EnsemblBacteria; AAT43196; AAT43196; PTO0611.
DR   GeneID; 2844844; -.
DR   KEGG; pto:PTO0611; -.
DR   eggNOG; COG0112; -.
DR   HOGENOM; HOG000239403; -.
DR   KO; K00600; -.
DR   OMA; LEEWNID; -.
DR   BioCyc; PTOR263820:GHA3-633-MONOMER; -.
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:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP.
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    433       Serine hydroxymethyltransferase.
FT                                /FTId=PRO_0000113718.
FT   REGION      125    127       Substrate binding (By similarity).
FT   BINDING      35     35       Pyridoxal phosphate (By similarity).
FT   BINDING      55     55       Pyridoxal phosphate (By similarity).
FT   BINDING      57     57       Substrate (By similarity).
FT   BINDING      64     64       Substrate (By similarity).
FT   BINDING      65     65       Pyridoxal phosphate (By similarity).
FT   BINDING      99     99       Pyridoxal phosphate (By similarity).
FT   BINDING     121    121       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     176    176       Pyridoxal phosphate (By similarity).
FT   BINDING     204    204       Pyridoxal phosphate (By similarity).
FT   BINDING     230    230       Pyridoxal phosphate (By similarity).
FT   BINDING     366    366       Pyridoxal phosphate (By similarity).
FT   MOD_RES     231    231       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   433 AA;  48545 MW;  7667E9DD660C2278 CRC64;
     MLDNKKEYLK DAMFIRDMAM QHEQLFRESI PLIASENIMS PLAMEMLLTD LGFRYAEGLP
     HHRYYQGNEY VDVIEDKTTE LGKRLFNSKT FDPRPLSGTN ANMAVLYALT EPGDKISVPP
     LSGGGHISAA KFGAVGFRGL KTVQYPFDIN EMNIDIDGTI KTIKNERPKV CWFGQSVFLF
     PTPLKELQDA FNEVNARVVY DGAHVAGLIA GGEFQDPLRE GAEIITGSTH KTLPGPQHGM
     IIGNTDDDTW KKVQRGVFPG TLSNHHLNAM AALGVTLAEE LDFGRDYAKQ IVKNARHLGE
     KLYEFGFNVL GEKNGFTRSH TLAVDVSKNG GGRKVAENLE KSGIILNKNL LPWDDNKNSQ
     NPSGIRIGVQ EITRIGFMED DVTELAEILR DAVINEKPVN EIRRRALELK SRFNNIEYCY
     GNMKPYSYIK IFE
//
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