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Phosphoserine aminotransferase (PSAT) (EC 2.6.1.52) (Endometrial progesterone-induced protein) (EPIP) (Phosphohydroxythreonine aminotransferase)

 SERC_RABIT              Reviewed;         370 AA.
P10658;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
28-FEB-2018, entry version 123.
RecName: Full=Phosphoserine aminotransferase;
Short=PSAT;
EC=2.6.1.52;
AltName: Full=Endometrial progesterone-induced protein;
Short=EPIP;
AltName: Full=Phosphohydroxythreonine aminotransferase;
Name=PSAT1; Synonyms=PSA;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3651428; DOI=10.1021/bi00387a035;
Misrahi M., Atger M., Milgrom E.;
"A novel progesterone-induced messenger RNA in rabbit and human
endometria. Cloning and sequence analysis of the complementary DNA.";
Biochemistry 26:3975-3982(1987).
[2]
POSSIBLE FUNCTION.
PubMed=2682527; DOI=10.1093/nar/17.20.8379;
van der Zel A., Lam H.-M., Winkler M.E.;
"Extensive homology between the Escherichia coli K-12 SerC(PdxF)
aminotransferase and a protein encoded by a progesterone-induced mRNA
in rabbit and human endometria.";
Nucleic Acids Res. 17:8379-8379(1989).
-!- FUNCTION: Catalyzes the reversible conversion of 3-
phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
phosphonooxybutanoate to phosphohydroxythreonine.
{ECO:0000269|PubMed:2682527}.
-!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3-
phosphonooxypyruvate + L-glutamate.
-!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate =
(3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250};
-!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
from 3-phospho-D-glycerate: step 2/3.
-!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
phosphate: step 3/5.
-!- SUBUNIT: Homodimer.
-!- INDUCTION: By progesterone.
-!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
aminotransferase family. SerC subfamily. {ECO:0000305}.
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EMBL; M17099; AAA31245.1; -; mRNA.
PIR; A26998; A26998.
RefSeq; NP_001075740.1; NM_001082271.1.
UniGene; Ocu.1872; -.
ProteinModelPortal; P10658; -.
SMR; P10658; -.
STRING; 9986.ENSOCUP00000006706; -.
PRIDE; P10658; -.
GeneID; 100009099; -.
KEGG; ocu:100009099; -.
CTD; 29968; -.
eggNOG; KOG2790; Eukaryota.
eggNOG; COG1932; LUCA.
HOGENOM; HOG000088965; -.
HOVERGEN; HBG001218; -.
InParanoid; P10658; -.
KO; K00831; -.
UniPathway; UPA00135; UER00197.
UniPathway; UPA00244; UER00311.
Proteomes; UP000001811; Unplaced.
GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
CDD; cd00611; PSAT_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
HAMAP; MF_00160; SerC_aminotrans_5; 1.
InterPro; IPR000192; Aminotrans_V_dom.
InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
InterPro; IPR022278; Pser_aminoTfrase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
Pfam; PF00266; Aminotran_5; 1.
PIRSF; PIRSF000525; SerC; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR01364; serC_1; 1.
PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
2: Evidence at transcript level;
Acetylation; Amino-acid biosynthesis; Aminotransferase;
Complete proteome; Phosphoprotein; Pyridoxal phosphate;
Reference proteome; Serine biosynthesis; Transferase.
CHAIN 1 370 Phosphoserine aminotransferase.
/FTId=PRO_0000150137.
REGION 79 80 Pyridoxal phosphate binding.
{ECO:0000250}.
REGION 241 242 Pyridoxal phosphate binding.
{ECO:0000250}.
BINDING 45 45 L-glutamate. {ECO:0000250}.
BINDING 107 107 Pyridoxal phosphate. {ECO:0000250}.
BINDING 156 156 Pyridoxal phosphate. {ECO:0000250}.
BINDING 176 176 Pyridoxal phosphate. {ECO:0000250}.
BINDING 199 199 Pyridoxal phosphate. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9Y617}.
MOD_RES 51 51 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y617}.
MOD_RES 127 127 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99K85}.
MOD_RES 200 200 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
MOD_RES 269 269 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y617}.
MOD_RES 318 318 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y617}.
MOD_RES 323 323 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y617}.
MOD_RES 331 331 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y617}.
MOD_RES 333 333 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y617}.
SEQUENCE 370 AA; 40621 MW; 7AB3A6E6B2D4085F CRC64;
MDSPRQIVNF GPGPAKLPHS VLLEIQKELL DYKGLGISVL EMSHRSSDFA KIVNNTENLV
RELLAVPDNY KVIFLQGGGC GQFSAVPLNL IGLKPGRCAD YVVTGAWSAK AAEEAKKFGT
VNIVHPKLGS YTKIPDPSTW NLNPDASYVY YCANETVHGV EFDFVPDVKG AILVCDMSSN
FLSRPVDVSK FGVIFAGAQK NVGAAGVTVV IVRDDLLGFA LRECPSVLEY KVQATSSSLY
NTPPCFSIYV MGLVLEWIKN NGGAAAMKKL STIKSQMIYE IIDNSQGFYV CPVEPRNRSM
MNIPFRIGNA KGDEALEKRF LDKALELHMI SLKGHRSVGG VRVSLYNAVT IEDVQKLASF
MKNFLEMHQL


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