(data stored in ACNUC7421 zone)

EMBL: AM286690.HISC-1

AM286690.HISC-1      Location/Qualifiers
FT   CDS             620582..621709
FT                   /transl_table=11
FT                   /gene="hisC-1"
FT                   /locus_tag="ABO_0563"
FT                   /product="histidinol-phosphate aminotransferase"
FT                   /function="Histidinol-phosphate aminotransferase is a
FT                   pyridoxal 5'-phosphate (PLP)-dependent enzyme catalyzing a
FT                   reversible transamination reaction between histidinol
FT                   phosphate and 2-oxoglutarate to form imidazole acetol
FT                   phosphate and glutamate. L-histidinol-phosphate +
FT                   2-oxoglutarate = 3- (imidazol-4-yl)-2-oxopropyl phosphate +
FT                   L-glutamate."
FT                   /EC_number="2.6.1.9"
FT                   /note="(histidinol-phosphate aminotransferase, imidazole
FT                   acetol-phosphate transaminase) identified by sequence
FT                   similarity; putative identified by match to PFAM protein
FT                   family HMMPF00155 InterPro: Aminotransferases class-I"
FT                   /note="High confidence in function and specificity"
FT                   /db_xref="EnsemblGenomes-Gn:ABO_0563"
FT                   /db_xref="EnsemblGenomes-Tr:CAL16011"
FT                   /db_xref="GOA:Q0VS37"
FT                   /db_xref="InterPro:IPR001917"
FT                   /db_xref="InterPro:IPR004839"
FT                   /db_xref="InterPro:IPR005861"
FT                   /db_xref="InterPro:IPR015421"
FT                   /db_xref="InterPro:IPR015422"
FT                   /db_xref="InterPro:IPR015424"
FT                   /db_xref="UniProtKB/TrEMBL:Q0VS37"
FT                   /inference="protein motif:HMMPFAM:HMMPF00155"
FT                   /protein_id="CAL16011.1"
FT                   /translation="MSKYWSDFVHHLEPYVPGEQPKMDKLVKLNTNEHPLGPSPKVIEA
FT                   IRGEVDDRLRLYPDPDSSQLKQAIADYYSGLGYGIKRSQVFVGNGSDEVLAHLFMGFFK
FT                   QHQPLLFPDITYSFYKVYCGLYQIDYQPVPLDDALGIAVDDYLEGDKPRANGGIIFPNP
FT                   NAPTGKLLPLSEIERLLQANTQTLVVIDEAYIDFAGPQGQGGATAIALVNRYPNLLVTQ
FT                   TLSKSRSLAGLRIGLAIGDGALIDGLNRIKDSFNSYPLDRLAIAAGVAAFKDQEWFEKG
FT                   CEQVIMQREWLNEQLGQRGFESLPSAANFLFTRHEQHSGLSLAQGLREQGIIVRHFGKP
FT                   ERIADYLRITIGTPEQNQALIVALDGLISKWKNAG"
     MSKYWSDFVH HLEPYVPGEQ PKMDKLVKLN TNEHPLGPSP KVIEAIRGEV DDRLRLYPDP        60
     DSSQLKQAIA DYYSGLGYGI KRSQVFVGNG SDEVLAHLFM GFFKQHQPLL FPDITYSFYK       120
     VYCGLYQIDY QPVPLDDALG IAVDDYLEGD KPRANGGIIF PNPNAPTGKL LPLSEIERLL       180
     QANTQTLVVI DEAYIDFAGP QGQGGATAIA LVNRYPNLLV TQTLSKSRSL AGLRIGLAIG       240
     DGALIDGLNR IKDSFNSYPL DRLAIAAGVA AFKDQEWFEK GCEQVIMQRE WLNEQLGQRG       300
     FESLPSAANF LFTRHEQHSG LSLAQGLREQ GIIVRHFGKP ERIADYLRIT IGTPEQNQAL       360
     IVALDGLISK WKNAG                                                        375
//

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