ID   HIS82_PSEF5             Reviewed;         370 AA.
AC   Q4K8N0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=PFL_4311;
OS   Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
CC   -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3-
CC       (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily.
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DR   EMBL; CP000076; AAY93566.1; -; Genomic_DNA.
DR   RefSeq; YP_261403.1; -.
DR   GeneID; 3478434; -.
DR   GenomeReviews; CP000076_GR; PFL_4311.
DR   KEGG; pfl:PFL_4311; -.
DR   NMPDR; fig|220664.3.peg.6123; -.
DR   HOGENOM; Q4K8N0; -.
DR   OMA; Q4K8N0; KGYIVRS.
DR   BioCyc; PFLU220664:PFL_4311-MON; -.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01023; -; 1.
DR   InterPro; IPR004839; Aminotrans_I/II.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   TIGRFAMs; TIGR01141; hisC; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Histidine biosynthesis; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    370       Histidinol-phosphate aminotransferase 2.
FT                                /FTId=PRO_0000153420.
FT   MOD_RES     230    230       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   370 AA;  39894 MW;  21FE003953A5637A CRC64;
     MSGDFLALAQ PGVQQLSPYV PGKPVDELAR ELDIDPATIV KLASNENPLG ASPKALAAIR
     DELAELTRYP DGNGFALKSL LAERCGVEID QVTLGNGSND ILELVARAYL APGLNAVFSE
     HAFAVYPIVT QAVGAQARVV PAKNWGHDLP AMLKAIDDRT RVVFIANPNN PTGTWFGAEE
     LDEFLQDVPA HVLVVLDEAY IEYAEGSDLP DGLDFLAAYP NLLVSRTFSK AYGLAALRVG
     YGLSTPVVAD VLNRVRQPFN VNSLALAAAC AALEDVDYLA ESRRLNEAGM QQLEAGFRDL
     GLRWIPSKGN FIAVDLGREA APIFQELLRE GVIVRPVANY GMPNHLRITI GLPAENTRFL
     EALAKVLARA
//