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Database: UniProt
Entry: E2SDG4_9ACTN
LinkDB: E2SDG4_9ACTN
Original site: E2SDG4_9ACTN 
ID   E2SDG4_9ACTN            Unreviewed;       368 AA.
AC   E2SDG4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Phosphoserine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
DE            EC=2.6.1.52 {ECO:0000256|HAMAP-Rule:MF_00160};
DE   AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
DE            Short=PSAT {ECO:0000256|HAMAP-Rule:MF_00160};
GN   Name=serC {ECO:0000256|HAMAP-Rule:MF_00160};
GN   ORFNames=HMPREF0063_11750 {ECO:0000313|EMBL:EFQ82541.1};
OS   Aeromicrobium marinum DSM 15272.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=585531 {ECO:0000313|EMBL:EFQ82541.1, ECO:0000313|Proteomes:UP000003111};
RN   [1] {ECO:0000313|EMBL:EFQ82541.1, ECO:0000313|Proteomes:UP000003111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15272 {ECO:0000313|EMBL:EFQ82541.1,
RC   ECO:0000313|Proteomes:UP000003111};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC       phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC       phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000256|HAMAP-
CC       Rule:MF_00160}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC         oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC         ChEBI:CHEBI:58538; EC=2.6.1.52;
CC         Evidence={ECO:0000256|ARBA:ARBA00001607, ECO:0000256|HAMAP-
CC         Rule:MF_00160};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC         L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC         Evidence={ECO:0000256|ARBA:ARBA00001871, ECO:0000256|HAMAP-
CC         Rule:MF_00160};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00160};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00160};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 2/3. {ECO:0000256|ARBA:ARBA00005099,
CC       ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC       {ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily.
CC       {ECO:0000256|ARBA:ARBA00006904, ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFQ82541.1}.
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DR   EMBL; ACLF03000006; EFQ82541.1; -; Genomic_DNA.
DR   RefSeq; WP_007076842.1; NZ_CM001024.1.
DR   AlphaFoldDB; E2SDG4; -.
DR   STRING; 585531.HMPREF0063_11750; -.
DR   eggNOG; COG1932; Bacteria.
DR   HOGENOM; CLU_061974_0_0_11; -.
DR   OrthoDB; 975012at2; -.
DR   UniPathway; UPA00135; UER00197.
DR   UniPathway; UPA00244; UER00311.
DR   Proteomes; UP000003111; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR006272; Pser_aminoTfrase_mycobac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01366; serC_3; 1.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   PANTHER; PTHR21152:SF24; SERINE--PYRUVATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00160};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW   Rule:MF_00160}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00160}; Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003111};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299, ECO:0000256|HAMAP-
KW   Rule:MF_00160};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000313|EMBL:EFQ82541.1}.
FT   DOMAIN          134..328
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   BINDING         42
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         100
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         146
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         169
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         192
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   BINDING         244..245
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT   MOD_RES         193
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
SQ   SEQUENCE   368 AA;  39073 MW;  6C5B8842DC41CA14 CRC64;
     MKIPADLLPR DGRFGSGPSK VRPEALAALA ASGSSLMGTS HRQPPVKQLV GRLREGLAQL
     FTLPDGYEVV LGLGGSHAFW DAATFGLVSE RSQHLVHGEF TAKFAAATTA APFLADPDVV
     ESAFSTRPSP RAVAGVDVYA WAHNETSTGV MAPVERVADA DDGALVLVDA TSGAGGLPVD
     VSQTDAYYFA PQKSFASDGG LWVALMSPAA IERAERIKAE GRYVPAFLDL PTAIDNSRKD
     QTYNTPAVAT LFLMEHQVRW LNGLGGLDAA VGRTTESSGR LYAWAERTSY VTPFVPDPAD
     RSLVVGTLDL DGVDAAAVAG VLRENGIVDV DGYRGLKRNQ LRIAMFPAID PDDVTALTRC
     IDHVVDRL
//
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