SERC_ALKAL
ID SERC_ALKAL Reviewed; 361 AA.
AC Q9RME2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
DE Short=PSAT;
GN Name=serC;
OS Alkalihalobacillus alcalophilus (Bacillus alcalophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=1445;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27647 / DSM 485 / JCM 5262 / NBRC 15653 / NCTC 4553 / 1;
RA Battchikova N.V., Koivulehto M.K.;
RT "Phosphoserine aminotransferase from obligate alkalophile Bacillus
RT alcalophilus.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBUNIT, AND CRYSTALLIZATION.
RC STRAIN=ATCC 27647 / DSM 485 / JCM 5262 / NBRC 15653 / NCTC 4553 / 1;
RX PubMed=14646107; DOI=10.1107/s0907444903021231;
RA Dubnovitsky A.P., Kapetaniou E.G., Papageorgiou A.C.;
RT "Expression, purification, crystallization and preliminary crystallographic
RT analysis of phosphoserine aminotransferase from Bacillus alcalophilus.";
RL Acta Crystallogr. D 59:2319-2321(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) IN COMPLEX WITH PLP, SUBUNIT,
RP COFACTOR, AND PH DEPENDENCE.
RC STRAIN=ATCC 27647 / DSM 485 / JCM 5262 / NBRC 15653 / NCTC 4553 / 1;
RX PubMed=15608117; DOI=10.1110/ps.041029805;
RA Dubnovitsky A.P., Kapetaniou E.G., Papageorgiou A.C.;
RT "Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of
RT phosphoserine aminotransferase from Bacillus alcalophilus.";
RL Protein Sci. 14:97-110(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH PLP, AND COFACTOR.
RC STRAIN=ATCC 27647 / DSM 485 / JCM 5262 / NBRC 15653 / NCTC 4553 / 1;
RX PubMed=15883191; DOI=10.1110/ps.051397905;
RA Dubnovitsky A.P., Ravelli R.B.G., Popov A.N., Papageorgiou A.C.;
RT "Strain relief at the active site of phosphoserine aminotransferase induced
RT by radiation damage.";
RL Protein Sci. 14:1498-1507(2005).
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:0000269|PubMed:14646107}.
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 -!- 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:15608117, ECO:0000269|PubMed:15883191};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000269|PubMed:15608117, ECO:0000269|PubMed:15883191};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0. At pH 9.5, retains more than 60% of its maximum
CC activity. At pH 7.0 the relative activity is less than 10%.
CC {ECO:0000269|PubMed:15608117};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14646107,
CC ECO:0000269|PubMed:15608117, ECO:0000269|PubMed:15883191}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF204962; AAF13453.1; -; Genomic_DNA.
DR PDB; 1W23; X-ray; 1.08 A; A/B=2-361.
DR PDB; 2BHX; X-ray; 1.68 A; A/B=2-361.
DR PDB; 2BI1; X-ray; 1.69 A; A/B=2-361.
DR PDB; 2BI2; X-ray; 1.69 A; A/B=2-361.
DR PDB; 2BI3; X-ray; 1.69 A; A/B=2-361.
DR PDB; 2BI5; X-ray; 1.73 A; A/B=2-361.
DR PDB; 2BI9; X-ray; 1.73 A; A/B=2-361.
DR PDB; 2BIA; X-ray; 1.77 A; A/B=2-361.
DR PDB; 2BIE; X-ray; 1.30 A; A/B=1-361.
DR PDB; 2BIG; X-ray; 1.30 A; A/B=1-361.
DR PDB; 4AZJ; X-ray; 1.50 A; A/B=2-361.
DR PDB; 4AZK; X-ray; 1.60 A; A/B=2-361.
DR PDBsum; 1W23; -.
DR PDBsum; 2BHX; -.
DR PDBsum; 2BI1; -.
DR PDBsum; 2BI2; -.
DR PDBsum; 2BI3; -.
DR PDBsum; 2BI5; -.
DR PDBsum; 2BI9; -.
DR PDBsum; 2BIA; -.
DR PDBsum; 2BIE; -.
DR PDBsum; 2BIG; -.
DR PDBsum; 4AZJ; -.
DR PDBsum; 4AZK; -.
DR AlphaFoldDB; Q9RME2; -.
DR SMR; Q9RME2; -.
DR DrugBank; DB02327; Triethylene glycol.
DR PRIDE; Q9RME2; -.
DR BRENDA; 2.6.1.52; 628.
DR UniPathway; UPA00135; UER00197.
DR EvolutionaryTrace; Q9RME2; -.
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; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43247; PTHR43247; 1.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW Pyridoxal phosphate; Serine biosynthesis; Transferase.
FT CHAIN 1..361
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000293583"
FT BINDING 43
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 77..78
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 103
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 153
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 173
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 196
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT BINDING 238..239
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 45..62
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:1W23"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1W23"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:1W23"
FT TURN 195..199
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:1W23"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 260..280
FT /evidence="ECO:0007829|PDB:1W23"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 307..319
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:1W23"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:1W23"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:1W23"
FT HELIX 344..360
FT /evidence="ECO:0007829|PDB:1W23"
SQ SEQUENCE 361 AA; 40335 MW; C4D48D1785C60A85 CRC64;
MVKQVFNFNA GPSALPKPAL ERAQKELLNF NDTQMSVMEL SHRSQSYEEV HEQAQNLLRE
LLQIPNDYQI LFLQGGASLQ FTMLPMNLLT KGTIGNYVLT GSWSEKALKE AKLLGETHIA
ASTKANSYQS IPDFSEFQLN ENDAYLHITS NNTIYGTQYQ NFPEINHAPL IADMSSDILS
RPLKVNQFGM IYAGAQKNLG PSGVTVVIVK KDLLNTKVEQ VPTMLQYATH IKSDSLYNTP
PTFSIYMLRN VLDWIKDLGG AEAIAKQNEE KAKIIYDTID ESNGFYVGHA EKGSRSLMNV
TFNLRNEELN QQFLAKAKEQ GFVGLNGHRS VGGCRASIYN AVPIDACIAL RELMIQFKEN
A
