ID   HIS81_ANAVT             Reviewed;         350 AA.
AC   Q3M504;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   26-MAY-2009, entry version 21.
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=Ava_4334;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-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; CP000117; ABA23932.1; -; Genomic_DNA.
DR   RefSeq; YP_324827.1; -.
DR   GeneID; 3680768; -.
DR   GenomeReviews; CP000117_GR; Ava_4334.
DR   KEGG; ava:Ava_4334; -.
DR   NMPDR; fig|240292.3.peg.4579; -.
DR   HOGENOM; Q3M504; -.
DR   OMA; Q3M504; SIVIRAC.
DR   BioCyc; AVAR240292:AVA_4334-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    350       Histidinol-phosphate aminotransferase 1.
FT                                /FTId=PRO_0000230203.
FT   MOD_RES     211    211       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   350 AA;  38720 MW;  9B2007867C9065E8 CRC64;
     MTNYFRSNVE AMASYVPGEQ PPRGTQVIKL NSNENPYPPS PAALAALQDI DGEWLRRYPE
     PLGGEFREAA SKVLGVPSDW LIVGNGSDEI LSIVIRACTE PGRKVVYPMP TYVLYRTLTQ
     MQAADILEIP YQENNVLPVA ELIAADGAVT FIASPNSPSG HIVPNDDLRK LASELSGVLV
     IDEAYVDFAE ESALDLVQEY ENVILIRTLS KGYSLAGLRL GFGVGNPKLL DGLFKVKDSY
     NIDAIACKVA AVAITDQAYK NSCVAKVKAS RTQLTKDLKQ LGFHVWDSHG NFLLTKPPEG
     NAEYLYEKLK EQKILIRYFQ QPGLEDKLRI TVGTDEQNHI LVRALRDLLR
//