ID G0CUY8_CORUB Unreviewed; 343 AA.
AC G0CUY8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 01-MAY-2013, entry version 15.
DE SubName: Full=Putative uncharacterized protein;
GN OrderedLocusNames=CULC22_00165;
OS Corynebacterium ulcerans (strain BR-AD22).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=945712;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR-AD22;
RX PubMed=21801446; DOI=10.1186/1471-2164-12-383;
RA Trost E., Al-Dilaimi A., Papavasiliou P., Schneider J., Viehoever P.,
RA Burkovski A., Soares S.C., Almeida S.S., Dorella F.A., Miyoshi A.,
RA Azevedo V., Schneider M.P., Silva A., Santos C.S., Santos L.S.,
RA Sabbadini P., Dias A.A., Hirata R.Jr., Mattos-Guaraldi A.L., Tauch A.;
RT "Comparative analysis of two complete Corynebacterium ulcerans genomes
RT and detection of candidate virulence factors.";
RL BMC Genomics 12:383-383(2011).
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.
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DR EMBL; CP002791; AEG82883.1; -; Genomic_DNA.
DR RefSeq; YP_004628802.1; NC_015683.1.
DR EnsemblBacteria; AEG82883; AEG82883; CULC22_00165.
DR GeneID; 10842713; -.
DR KEGG; cul:CULC22_00165; -.
DR KO; K00817; -.
DR BioCyc; CULC945712:GHG6-168-MONOMER; -.
DR UniPathway; UPA00031; UER00012.
DR GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IEA:InterPro.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01023; HisC_aminotrans_2; 1; -.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
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; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW Histidine biosynthesis; Pyridoxal phosphate; Transferase.
SQ SEQUENCE 343 AA; 36966 MW; 70253A22C9793C09 CRC64;
MIREDLAQIP TYVPGHHADH TLKLSSNEVA FGPLPGAAEA MAKAATTVNR YPDMGAEEIR
KRLAEHLGLG TQQVAVGCGS SALCQQLVQI SAGPGDEVIF PWRSFEAYPI FVHVTGATPV
AVPLKEGFND LDAMAAAITE NTRLIFVCNP NNPTGTLISQ DAFLAFMNKV PSNVLVALDE
AYIEYARAED TPLATELIDA YPNLVGLRTF SKAFGLAGIR IGYAFGSPRL IEALNKVALP
FGVNAVAQAG AIASLENLDE LMERTEEVVT NRDRVADHVG AGHSQANFVW IPADSRPESP
MEIAEQLRNH DVVVRAFPEG VRITVTNSEE TDRLLAAWDA SFS
//
