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 01-MAY-2013, entry version 63.
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; TEANFIF; -.
DR UniPathway; UPA00031; UER00012.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:HAMAP.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA: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; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR01141; hisC; 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 1 361 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
//
