HIS81_PSEAE
ID HIS81_PSEAE Reviewed; 351 AA.
AC Q9HVX0;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Histidinol-phosphate aminotransferase 1;
DE EC=2.6.1.9;
DE AltName: Full=Imidazole acetol-phosphate transaminase 1;
GN Name=hisC1; OrderedLocusNames=PA4447;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC ChEBI:CHEBI:57980; EC=2.6.1.9;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000305}.
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DR EMBL; AE004091; AAG07835.1; -; Genomic_DNA.
DR PIR; C83089; C83089.
DR RefSeq; NP_253137.1; NC_002516.2.
DR RefSeq; WP_003098833.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; Q9HVX0; -.
DR SMR; Q9HVX0; -.
DR STRING; 287.DR97_1625; -.
DR PaxDb; Q9HVX0; -.
DR PRIDE; Q9HVX0; -.
DR EnsemblBacteria; AAG07835; AAG07835; PA4447.
DR GeneID; 880991; -.
DR KEGG; pae:PA4447; -.
DR PATRIC; fig|208964.12.peg.4656; -.
DR PseudoCAP; PA4447; -.
DR HOGENOM; CLU_017584_3_0_6; -.
DR InParanoid; Q9HVX0; -.
DR OMA; FDGYPIL; -.
DR PhylomeDB; Q9HVX0; -.
DR BioCyc; PAER208964:G1FZ6-4535-MON; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR005861; HisP_aminotrans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..351
FT /note="Histidinol-phosphate aminotransferase 1"
FT /id="PRO_0000153417"
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 351 AA; 38655 MW; 585101ABA429DCC2 CRC64;
MSKFWSPFVK DLVPYVPGEQ PKLSRLVKLN TNENPYGPSP QALAAMQAEL NDDLRLYPDP
NGERLKQAVA AHYGVQANQV FVGNGSDEVL AHIFHGLFQH DLPLLFPDVT YSFYPVYCGL
YGIAHEKIAL DERFRIRVED YARPNGGIIF PNPNAPTGCL LPLDAIEAML KASPDSVVVV
DEAYVDFGGE SAIALVDRYP NLLVTQTLSK SRSLAGLRVG LAVGHADLVE ALERIKNSFN
SYPLDRLAIA GAAAAFEDDA YFRRTCQAVI DSREALSASL QALGFEVLPS AANFVFARHP
RHDAGQIAST LREQGVIVRH FKQARIDQFL RITIGSPEQN QALLDALHFL K