(data stored in SCRATCH zone)

SWISSPROT: C6WI30_ACTMD

ID   C6WI30_ACTMD            Unreviewed;       377 AA.
AC   C6WI30;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
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   OrderedLocusNames=Amir_0514 {ECO:0000313|EMBL:ACU34481.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34481.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34481.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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:SAAS00347519}.
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|SAAS:SAAS00635255}.
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
CC       from 3-phospho-D-glycerate: step 2/3. {ECO:0000256|HAMAP-
CC       Rule:MF_00160, ECO:0000256|SAAS:SAAS00635259}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_00160}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00160,
CC       ECO:0000256|SAAS:SAAS00347516}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160,
CC       ECO:0000256|SAAS:SAAS00347422}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00160, ECO:0000256|SAAS:SAAS00635246}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00160}.
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DR   EMBL; CP001630; ACU34481.1; -; Genomic_DNA.
DR   RefSeq; WP_012783144.1; NC_013093.1.
DR   STRING; 446462.Amir_0514; -.
DR   EnsemblBacteria; ACU34481; ACU34481; Amir_0514.
DR   KEGG; ami:Amir_0514; -.
DR   eggNOG; ENOG4107R8H; Bacteria.
DR   eggNOG; COG1932; LUCA.
DR   HOGENOM; HOG000239573; -.
DR   KO; K00831; -.
DR   OMA; ETDVYYF; -.
DR   OrthoDB; POG091H00RM; -.
DR   UniPathway; UPA00135; UER00197.
DR   UniPathway; UPA00244; UER00311.
DR   Proteomes; UP000002213; 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-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-HAMAP.
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; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR006272; Pser_aminoTfrase_mycobac.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01366; serC_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WI30.
DR   SWISS-2DPAGE; C6WI30.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00635287};
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00635261, ECO:0000313|EMBL:ACU34481.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00019693};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00635253};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Serine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00635251};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00160,
KW   ECO:0000256|SAAS:SAAS00635243, ECO:0000313|EMBL:ACU34481.1}.
FT   DOMAIN       26    336       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION      252    253       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
FT   BINDING      51     51       L-glutamate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00160}.
FT   BINDING     109    109       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     155    155       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     177    177       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   BINDING     200    200       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00160}.
FT   MOD_RES     201    201       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00160}.
SQ   SEQUENCE   377 AA;  40206 MW;  8F1BA26E541A7128 CRC64;
     MTQTADPTSL VLPADLKPSD GRFGCGPSKV RPEALRALAA EGADLMGTSH RQKPVKSLVG
     EVRSGLRALF SLPEGYEVVL GNGGTTAFWD AAAFGLVRER SQHFTYGEFS SKFAKVTKDA
     PFLGEPVVVK SEPGTAPEIT FAEGVDLVGW AHNETSTGVA VPVSRPAGSD GALVAIDATS
     GAGGLPVKAE DFDVYYFAPQ KCFASDGGLW LSLMSPAALD RVREIGASGR WVPEFLSLTT
     ALDNSTKDQT YNTPSVATLF LLNEQLKWLN GNGGLDWAVS RTADSSSRLY SWAEQTSYTS
     PYVADPAHRS QVVGTVDFAD EVDASVVAKV LRANGIVDVE PYRKLGRNQL RVAMFPAVEP
     EDVSTLTEAV DWVVGQL
//

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