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Database: UniProt
Entry: B9Y9U2_9FIRM
LinkDB: B9Y9U2_9FIRM
Original site: B9Y9U2_9FIRM 
ID   B9Y9U2_9FIRM            Unreviewed;       370 AA.
AC   B9Y9U2;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   28-MAR-2018, entry version 64.
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   ECO:0000313|EMBL:EEF67252.1};
GN   ORFNames=HOLDEFILI_02599 {ECO:0000313|EMBL:EEF67252.1};
OS   Holdemania filiformis DSM 12042.
OC   Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Holdemania.
OX   NCBI_TaxID=545696 {ECO:0000313|EMBL:EEF67252.1, ECO:0000313|Proteomes:UP000005950};
RN   [1] {ECO:0000313|EMBL:EEF67252.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF67252.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H.,
RA   Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEF67252.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF67252.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M.,
RA   Liep D., Gordon J.;
RT   "Draft genome sequence of Holdemania filiformis DSM 12042.";
RL   Submitted (FEB-2009) 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.
CC       {ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000256|SAAS:SAAS00635267}.
CC   -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate =
CC       (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000256|SAAS:SAAS00635249}.
CC   -!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3-
CC       phosphonooxypyruvate + L-glutamate. {ECO:0000256|HAMAP-
CC       Rule:MF_00160, ECO:0000256|RuleBase:RU004505,
CC       ECO:0000256|SAAS:SAAS00635255}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 2/3. {ECO:0000256|HAMAP-
CC       Rule:MF_00160, ECO:0000256|RuleBase:RU004505,
CC       ECO:0000256|SAAS:SAAS00635259}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00160,
CC       ECO:0000256|SAAS:SAAS00635271}.
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|SAAS:SAAS00635246}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EEF67252.1}.
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DR   EMBL; ACCF01000155; EEF67252.1; -; Genomic_DNA.
DR   STRING; 545696.HOLDEFILI_02599; -.
DR   EnsemblBacteria; EEF67252; EEF67252; HOLDEFILI_02599.
DR   eggNOG; ENOG4107QM1; Bacteria.
DR   eggNOG; COG1932; LUCA.
DR   OrthoDB; POG091H01K1; -.
DR   UniPathway; UPA00135; UER00197.
DR   Proteomes; UP000005950; Unassembled WGS sequence.
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   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01364; serC_1; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|RuleBase:RU004505, ECO:0000256|SAAS:SAAS00635287};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|RuleBase:RU004505, ECO:0000256|SAAS:SAAS00635261,
KW   ECO:0000313|EMBL:EEF67252.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005950};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00635955};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005950};
KW   Serine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|RuleBase:RU004505, ECO:0000256|SAAS:SAAS00635251};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|RuleBase:RU004505, ECO:0000256|SAAS:SAAS00635243,
KW   ECO:0000313|EMBL:EEF67252.1}.
FT   DOMAIN       14    356       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION       86     87       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
FT   REGION      244    245       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
FT   BINDING      52     52       L-glutamate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00160}.
FT   BINDING     112    112       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     160    160       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     180    180       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     203    203       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   MOD_RES     204    204       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
SQ   SEQUENCE   370 AA;  40909 MW;  9B672B2A5621ED89 CRC64;
     MGILEKRMTT MTRVFNFSAG PSQLPTEVLQ KCAAELMEYG ISGQSVMEMS HRSSSFLEII
     ETTERRLSSL LQIPESYQVL FLQGGASLQF TMVPMNLLKP GGKAGVIHTG AWTKKAIAEC
     RKIGGCEILA SSEAEHFTSI PKGVTIPQDL DYVHICENNT IYGTKYKELP ECGSVPLVAD
     CSSCILSEPM EISRYGLIFA GAQKNMGIAG LTVVIVREDL IQERPEIPSM LSYAVQAKNK
     SMFNTPPTFA IYLLGLVLEW IENRYHDLAA LKTVNQQKAA LLYDQIDQSR LFTNPVRPED
     RSIMNVPFVT GDAALDAKFI AAAEAEGLVN LKGHRSVGGM RASIYNAMPL EGVQKLVDLM
     RRFEEENRIC
//
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