ID   HIS81_THIDA             Reviewed;         384 AA.
AC   Q3SK85;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=Tbd_0952;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Hydrogenophilales;
OC   Hydrogenophilaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic,
RT   facultatively anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ96905.1; -; Genomic_DNA.
DR   RefSeq; YP_314710.1; -.
DR   GeneID; 3672744; -.
DR   GenomeReviews; CP000116_GR; Tbd_0952.
DR   KEGG; tbd:Tbd_0952; -.
DR   NMPDR; fig|292415.3.peg.542; -.
DR   HOGENOM; Q3SK85; -.
DR   OMA; Q3SK85; KGYIVRS.
DR   BioCyc; TDEN292415:TBD_0952-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    384       Histidinol-phosphate aminotransferase 1.
FT                                /FTId=PRO_0000153471.
FT   MOD_RES     233    233       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   384 AA;  40437 MW;  A3457C4415E77AA1 CRC64;
     MSGCDSICAA TAPPHVRAIA PYQPGKPISE LARELGLAEA DIVKLASNEN PLGPSPFALA
     AAQDALLDMA LYPDGAGYAL KAKLSARLGV DAAQIVLGNG SNDVLDMVAR AYLAPGTSAV
     YAQYAFAVYP IATHTVGAHG IAVAARDFGH DLERMRAAIR DDTRVVWIAN PNNPTGTFLP
     WNEIEAFLET VPPRVLVVLD EAYGEYLAPA SRCDTAAWVV RFPNLLISRT FSKAYGLAGL
     RVGYGIGHAD VVDLLNRVRH PFNVNASALA AAEAALDDDA FLARSYALNA AGMQQLLGGL
     AALDIETVPS KGNFVLARVG DAARINTELL KRGVIVRPVA AYGLPEFLRV SVGLAGQNAR
     FLDALGEVLA AAPGRHPDSR KALP
//