SERC_PSEAE
ID SERC_PSEAE Reviewed; 361 AA.
AC Q9HZ66;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Phosphoserine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160};
DE EC=2.6.1.52 {ECO:0000255|HAMAP-Rule:MF_00160};
DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160};
DE Short=PSAT {ECO:0000255|HAMAP-Rule:MF_00160};
GN Name=serC {ECO:0000255|HAMAP-Rule:MF_00160}; OrderedLocusNames=PA3167;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000255|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:0000255|HAMAP-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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00160};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00160};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00160}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00160}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00160}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00160}.
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DR EMBL; AE004091; AAG06555.1; -; Genomic_DNA.
DR PIR; H83250; H83250.
DR RefSeq; NP_251857.1; NC_002516.2.
DR RefSeq; WP_003106701.1; NZ_QZGE01000023.1.
DR PDB; 4XK1; X-ray; 2.15 A; A/B=1-361.
DR PDBsum; 4XK1; -.
DR AlphaFoldDB; Q9HZ66; -.
DR SMR; Q9HZ66; -.
DR STRING; 287.DR97_4769; -.
DR PaxDb; Q9HZ66; -.
DR PRIDE; Q9HZ66; -.
DR DNASU; 882700; -.
DR EnsemblBacteria; AAG06555; AAG06555; PA3167.
DR GeneID; 882700; -.
DR KEGG; pae:PA3167; -.
DR PATRIC; fig|208964.12.peg.3310; -.
DR PseudoCAP; PA3167; -.
DR HOGENOM; CLU_034866_0_2_6; -.
DR InParanoid; Q9HZ66; -.
DR OMA; GYRASMY; -.
DR PhylomeDB; Q9HZ66; -.
DR BioCyc; PAER208964:G1FZ6-3227-MON; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00611; PSAT_like; 1.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase; Cytoplasm;
KW Pyridoxal phosphate; Pyridoxine biosynthesis; Reference proteome;
KW Serine biosynthesis; Transferase.
FT CHAIN 1..361
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150198"
FT BINDING 43
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 77..78
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 103
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 153
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 173
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 196
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT BINDING 238..239
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:4XK1"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 45..62
FT /evidence="ECO:0007829|PDB:4XK1"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:4XK1"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:4XK1"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:4XK1"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4XK1"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:4XK1"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:4XK1"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:4XK1"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4XK1"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:4XK1"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:4XK1"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 260..281
FT /evidence="ECO:0007829|PDB:4XK1"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:4XK1"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:4XK1"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:4XK1"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:4XK1"
FT HELIX 343..359
FT /evidence="ECO:0007829|PDB:4XK1"
SQ SEQUENCE 361 AA; 39949 MW; 9D787E60951018DF CRC64;
MSKRAFNFCA GPAALPDAVL QRAQAELLDW RGKGLSVMEM SHRSDDYVAI ASKAEQDLRD
LLDIPSDYKV LFLQGGASQQ FAEIPLNLLP EDGVADYIDT GIWSKKAIEE ARRYGTVNVA
ASAKEYDYFA IPGQNEWTLT KDAAYVHYAS NETIGGLEFD WIPETGDVPL VTDMSSDILS
RPLDVSRFGL IYAGAQKNIG PSGLVVVIVR EDLLGRARSV CPTMLNYKTA ADNGSMYNTP
ATYSWYLSGL VFEWLKEQGG VTAMEQRNRA KKDLLYKTID ASDFYTNPIQ PSARSWMNVP
FRLADERLDK PFLEGAEARG LLNLKGHRSV GGMRASIYNA LGLDAVEALV AYMAEFEKEH
G
