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Database: UniProt
Entry: Q67KI2
LinkDB: Q67KI2
Original site: Q67KI2 
ID   HIS8_SYMTH              Reviewed;         361 AA.
AC   Q67KI2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   14-MAY-2014, entry version 68.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisC; OrderedLocusNames=STH2831;
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Clostridiales Family XVIII. Incertae Sedis; Symbiobacterium.
OX   NCBI_TaxID=292459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863;
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T.,
RA   Morimura K., Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable
RT   bacterium that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD41816.1; -; Genomic_DNA.
DR   RefSeq; YP_076660.1; NC_006177.1.
DR   ProteinModelPortal; Q67KI2; -.
DR   STRING; 292459.STH2831; -.
DR   EnsemblBacteria; BAD41816; BAD41816; STH2831.
DR   GeneID; 2979869; -.
DR   KEGG; sth:STH2831; -.
DR   PATRIC; 23783843; VBISymThe116959_2810.
DR   eggNOG; COG0079; -.
DR   HOGENOM; HOG000288510; -.
DR   KO; K00817; -.
DR   OMA; GNFVMVD; -.
DR   OrthoDB; EOG6JMMWS; -.
DR   BioCyc; STHE292459:GJMM-2932-MONOMER; -.
DR   UniPathway; UPA00031; UER00012.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01141; hisC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Histidine biosynthesis; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    361       Histidinol-phosphate aminotransferase.
FT                                /FTId=PRO_0000153464.
FT   MOD_RES     221    221       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   361 AA;  39538 MW;  A025E063F67B970F CRC64;
     MSSVRTAVRR MKPYVPGKPV EDVQRELGLH DLVKLNQNEN PLGPSPRAVA AARAAMAQVH
     TYPEGTARRL RERLAQMWNL PADWFLIGNG SDEVFRLLAE VYLEPGDRVV VPEPSFAAYR
     FVAELMGAEV VAVPLAGWTM DLPAMAEAAA RGAKLLFLCR PNNPTGTVFA EADLRAALER
     VPPSTLVVVD EAYREFDETP FDSRALVQDY PNVVIARTFS KIYGMAGFRL GYGVMRPEVL
     APLYTARDPF SVNGLAVAAG LAALDDVEHV ERTRALTREG KAYLYAAFQR LGLGYVPSEA
     NFVLFDAGRP AAEVFDALLR RGVLVRPCGS FGLPDHLRVT VGTPEQNRRF VEALKAALGE
     G
//
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