ID   HIS82_PSYA2             Reviewed;         377 AA.
AC   Q4FQF9;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=Psyc_1901;
OS   Psychrobacter arcticus (strain DSM 17307 / 273-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   NASA Astrobiology Institute;
RA   Ayala-del-Rio H.L., Chain P., Ponder M.A., Di Bartolo G., Ivanova N.,
RA   Bergholz P.W., Hauser L., Land M., Bakermans C., Rodrigues D.,
RA   Klappenbach J.A., Zarka D., Larimer F., Richardson P., Thomashow M.F.,
RA   Tiedje J.M.;
RT   "Complete sequence of Psychrobacter arcticum 273-4.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000082; AAZ19749.1; -; Genomic_DNA.
DR   RefSeq; YP_265183.1; -.
DR   GeneID; 3515871; -.
DR   GenomeReviews; CP000082_GR; Psyc_1901.
DR   KEGG; par:Psyc_1901; -.
DR   NMPDR; fig|259536.4.peg.583; -.
DR   HOGENOM; Q4FQF9; -.
DR   OMA; Q4FQF9; DEQFQIR.
DR   BioCyc; PARC259536:PSYC_1901-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    377       Histidinol-phosphate aminotransferase 2.
FT                                /FTId=PRO_0000153427.
FT   MOD_RES     228    228       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   377 AA;  41304 MW;  026534B292523669 CRC64;
     MSESKIDNRL WSSKARNLSP YVPGEQPQHD DLCKLNTNEN PFPPSPKVGE AITKVLAQQA
     DDLRLYPAPE SEELRGALAA LYNLDINQVF VGNGSDEVLA LVFASFFLKN RPVLAPDISY
     SFYPVYANTF GIELVQIPLE ADFSISPDAY RRPCSGIIIA NPNAPTGLLL SLADIRKLAG
     EHSDSVIVID EAYIDFAQLE EASAESQMSA ISLINEFDNL LVTQTFSKSR SLAGLRVGMA
     FGNASLIEAL TRMKNSFNSY PLDKLAQAGA TASVLDVEYF EQTCQQVIDL RTSLTAELTA
     LGYDVLPSHA NFVFARPHDG AASQVAEVLR EQGIIVRHFD KPRINEYLRI TIGTPSQHER
     LINALKALQA VADVEAS
//