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Phosphoserine aminotransferase (EC 2.6.1.52) (Phosphohydroxythreonine aminotransferase) (PSAT)

 A0A1Q5ZY28_9SPHI        Unreviewed;       355 AA.
A0A1Q5ZY28;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
27-SEP-2017, entry version 4.
RecName: Full=Phosphoserine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
EC=2.6.1.52 {ECO:0000256|HAMAP-Rule:MF_00160};
AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
Short=PSAT {ECO:0000256|HAMAP-Rule:MF_00160};
Name=serC {ECO:0000256|HAMAP-Rule:MF_00160};
ORFNames=RG47T_2104 {ECO:0000313|EMBL:OKS86648.1};
Mucilaginibacter polytrichastri.
Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
Sphingobacteriaceae; Mucilaginibacter.
NCBI_TaxID=1302689 {ECO:0000313|EMBL:OKS86648.1, ECO:0000313|Proteomes:UP000186720};
[1] {ECO:0000313|EMBL:OKS86648.1, ECO:0000313|Proteomes:UP000186720}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RG4-7 {ECO:0000313|EMBL:OKS86648.1,
ECO:0000313|Proteomes:UP000186720};
Li Y.;
"Whole Genome Sequencing of Mucilaginibacter polytrichastri RG4-7(T)
isolated from the moss sample.";
Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the reversible conversion of 3-
phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
phosphonooxybutanoate to phosphohydroxythreonine.
{ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000256|SAAS:SAAS00635267}.
-!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate =
(3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.
{ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000256|SAAS:SAAS00635249}.
-!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3-
phosphonooxypyruvate + L-glutamate. {ECO:0000256|HAMAP-
Rule:MF_00160, ECO:0000256|RuleBase:RU004505,
ECO:0000256|SAAS:SAAS00635255}.
-!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
from 3-phospho-D-glycerate: step 2/3. {ECO:0000256|HAMAP-
Rule:MF_00160, ECO:0000256|RuleBase:RU004505,
ECO:0000256|SAAS:SAAS00635259}.
-!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_00160}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00160,
ECO:0000256|SAAS:SAAS00635271}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160}.
-!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
aminotransferase family. SerC subfamily.
{ECO:0000256|SAAS:SAAS00635246}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00160}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OKS86648.1}.
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EMBL; MPPL01000001; OKS86648.1; -; Genomic_DNA.
RefSeq; WP_074489306.1; NZ_MPPL01000001.1.
UniPathway; UPA00135; UER00197.
UniPathway; UPA00244; UER00311.
Proteomes; UP000186720; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
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.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160,
ECO:0000256|RuleBase:RU004505, ECO:0000256|SAAS:SAAS00635251};
Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160,
ECO:0000256|RuleBase:RU004505, ECO:0000256|SAAS:SAAS00635261,
ECO:0000313|EMBL:OKS86648.1};
Complete proteome {ECO:0000313|Proteomes:UP000186720};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00160,
ECO:0000256|SAAS:SAAS00635955};
Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160};
Reference proteome {ECO:0000313|Proteomes:UP000186720};
Serine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160,
ECO:0000256|RuleBase:RU004505, ECO:0000256|SAAS:SAAS00635251};
Transferase {ECO:0000256|HAMAP-Rule:MF_00160,
ECO:0000256|RuleBase:RU004505, ECO:0000256|SAAS:SAAS00635261,
ECO:0000313|EMBL:OKS86648.1}.
DOMAIN 4 337 Aminotran_5. {ECO:0000259|Pfam:PF00266}.
REGION 74 75 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00160}.
REGION 232 233 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_00160}.
BINDING 40 40 L-glutamate. {ECO:0000256|HAMAP-
Rule:MF_00160}.
BINDING 100 100 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00160}.
BINDING 148 148 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00160}.
BINDING 167 167 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00160}.
BINDING 190 190 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_00160}.
MOD_RES 191 191 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_00160}.
SEQUENCE 355 AA; 38792 MW; 194DE32A7895041B CRC64;
MKHNFGAGPG ILPHEVLKQA AEAVVNFNGI GLSVLEISHR SSEFEAVLDE AVKLVKELFS
VPDGYSVLFL QGGASTQFAM VPYNLLPQTG KAAYVESGVW ANKALKEAKY FGEVEVIATS
KESNFTYIPK DYSVPSDAAY LHLTSNNTIY GTQLHEFPAS SVPVICDMSS DIFSRKVNVA
DFGLIYAGAQ KNMGPAGVTL VIIKDDILGK ADRKIPAMFN YQTQIEGGSM YNTPPVFAIL
VSMLTLRWLK AKGGVEAIEK ENDAKAAALY TEIDRNPLFK GVSAVEDRSK MNVCFVVENP
EHEKPFLKLC DEKGIVGIKG HRSVGGFRAS IYNALPITSV HVLIETMQEF VEKNK


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