ID   HIS82_PSEAE             Reviewed;         369 AA.
AC   Q9HZ68;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Histidinol-phosphate aminotransferase 2;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase 2;
GN   Name=hisC2; OrderedLocusNames=PA3165;
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; AAG06553.1; -; Genomic_DNA.
DR   PIR; F83250; F83250.
DR   RefSeq; NP_251855.1; NC_002516.2.
DR   RefSeq; WP_003115433.1; NZ_QZGE01000023.1.
DR   AlphaFoldDB; Q9HZ68; -.
DR   SMR; Q9HZ68; -.
DR   STRING; 287.DR97_4771; -.
DR   PaxDb; Q9HZ68; -.
DR   PRIDE; Q9HZ68; -.
DR   DNASU; 882694; -.
DR   EnsemblBacteria; AAG06553; AAG06553; PA3165.
DR   GeneID; 882694; -.
DR   KEGG; pae:PA3165; -.
DR   PATRIC; fig|208964.12.peg.3308; -.
DR   PseudoCAP; PA3165; -.
DR   HOGENOM; CLU_017584_3_3_6; -.
DR   InParanoid; Q9HZ68; -.
DR   OMA; NYHVAGF; -.
DR   PhylomeDB; Q9HZ68; -.
DR   BioCyc; PAER208964:G1FZ6-3225-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..369
FT                   /note="Histidinol-phosphate aminotransferase 2"
FT                   /id="PRO_0000153418"
FT   MOD_RES         229
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   369 AA;  39483 MW;  CE912DC95699652E CRC64;
     MSDFLALAQP GVQKLSPYVP GKPVDELARE LGIDPAAIVK LASNENPLGA SPKALEAIRA
     ELAELTRYPD GNGFELKRKL AERCAVDAAQ VTLGNGSNDI LDLVARAYLA PGLNAVFSEH
     AFAVYPIATQ AVGAEGRAVK ARAWGHDLEA MLAAIDGQTR VVFVANPNNP TGTWFGADAL
     ERFLAQVPAE VLVVLDEAYI EYAEGDELPD GLDYLARHPN LLVSRTFSKA YGLASLRVGY
     ALSSKAVADV LNRVRQPFNV NSLALAAACA ALDDHDYLAQ SRRLNDSGMA QLEDGFHALG
     LSWIPSKGNF IAVDLARDAG PVYQALLREG VIVRPVAGYG MPTFLRVSIG LPEENDRFLQ
     ALGKVLAHD