SAT_THEMA
ID SAT_THEMA Reviewed; 384 AA.
AC Q9X1C0; G4FFD6;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Serine-pyruvate aminotransferase;
DE Short=SAT;
DE EC=2.6.1.51;
GN OrderedLocusNames=TM_1400; ORFNames=THEMA_07315, Tmari_1407;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RG DOE Joint Genome Institute;
RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18156253; DOI=10.1128/jb.01469-07;
RA Yang C., Rodionov D.A., Rodionova I.A., Li X., Osterman A.L.;
RT "Glycerate 2-kinase of Thermotoga maritima and genomic reconstruction of
RT related metabolic pathways.";
RL J. Bacteriol. 190:1773-1782(2008).
CC -!- FUNCTION: Involved in the degradation of L-serine via 3-
CC hydroxypyruvate. Catalyzes the transamination between L-serine and
CC pyruvate to yield 3-hydroxypyruvate and alanine.
CC {ECO:0000269|PubMed:18156253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine + pyruvate = 3-hydroxypyruvate + L-alanine;
CC Xref=Rhea:RHEA:22852, ChEBI:CHEBI:15361, ChEBI:CHEBI:17180,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57972; EC=2.6.1.51;
CC Evidence={ECO:0000269|PubMed:18156253};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36471.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL50331.1; -; Genomic_DNA.
DR EMBL; CP007013; AHD18704.1; -; Genomic_DNA.
DR PIR; A72257; A72257.
DR RefSeq; NP_229201.1; NC_000853.1.
DR RefSeq; WP_004081619.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X1C0; -.
DR SMR; Q9X1C0; -.
DR STRING; 243274.THEMA_07315; -.
DR EnsemblBacteria; AAD36471; AAD36471; TM_1400.
DR EnsemblBacteria; AGL50331; AGL50331; Tmari_1407.
DR KEGG; tma:TM1400; -.
DR KEGG; tmi:THEMA_07315; -.
DR KEGG; tmm:Tmari_1407; -.
DR KEGG; tmw:THMA_1429; -.
DR PATRIC; fig|243274.17.peg.1407; -.
DR eggNOG; COG0075; Bacteria.
DR InParanoid; Q9X1C0; -.
DR OMA; KNWLPIM; -.
DR OrthoDB; 996960at2; -.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IBA:GO_Central.
DR GO; GO:0004760; F:serine-pyruvate transaminase activity; IDA:UniProtKB.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..384
FT /note="Serine-pyruvate aminotransferase"
FT /id="PRO_0000428995"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 42106 MW; 3A23E83340A26290 CRC64;
MGKFLKKHYI MAPGPTPVPN DILTEGAKET IHHRTPQFVS IMEETLESAK YIFQTKHNVY
AFASTGTGAM EAAVANLVSP GDKVIVVVAG KFGERWRELC QAYGADIVEI ALEWGDAVTP
EQIEEALNKN PDAKVVFTTY SETSTGTVID LEGIARVTKE KDVVLVTDAV SALGAEPLKM
DEWGVDLVVT GSQKGLMLPP GLALISLNDK AWGLVEKSRS PRYYFDLRAY RKSYPDNPYT
PAVNMIYMLR KALQMIKEEG IENVWERHRI LGDATRAAVK ALGLELLSKR PGNVVTAVKV
PEGIDGKQIP KIMRDKYGVT IAGGQAKLKG KIFRIAHLGY MSPFDTITAI SALELTLKEL
GYEFELGVGV KAAEAVFAKE FIGE
