ID   HIS82_ANAVT             Reviewed;         380 AA.
AC   Q3MAX6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=Ava_2242;
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; ABA21860.1; -; Genomic_DNA.
DR   RefSeq; YP_322755.1; -.
DR   GeneID; 3679316; -.
DR   GenomeReviews; CP000117_GR; Ava_2242.
DR   KEGG; ava:Ava_2242; -.
DR   NMPDR; fig|240292.3.peg.2509; -.
DR   HOGENOM; Q3MAX6; -.
DR   OMA; Q3MAX6; SNRYPDG.
DR   BioCyc; AVAR240292:AVA_2242-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; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; FALSE_NEG.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Histidine biosynthesis; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    380       Histidinol-phosphate aminotransferase 2.
FT                                /FTId=PRO_0000230202.
FT   MOD_RES     236    236       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   380 AA;  41730 MW;  97124B9B0046E6C7 CRC64;
     MLPFIRSDLA QFTAYKPHPS SDTDAAVPAQ LDRLDTNESP CDLPPELKQK LAWTFQQVIE
     SNRYPDGGHE ELKDAIAQYV NESANISSSP ITAANISVGN GSDELIRSLL IATCLGAQGS
     ILVANPTFSM YGILAQTLGI PVVTVSRNPE NFEIDLTAAQ SAIEQTQNPP IRVVFVVHPN
     SPTANPLTTN ELRWLKSLSE QILVVVDEAY FEFSQTTLIS ELVQRPNWVI LRTFSKAFRL
     AAMRVGYCVA HPEAIAILEK VRLPYNLPSF SITSALVALQ NRAILLESIP QILNERAKLI
     TALSKYPELA VAESAANFIF LQLKTDNKNS PDTALLNLHQ QLKNSGTLVR QISGGLRITI
     GTPEENIRTL NHIQTALIKA
//