HIS81_BACAN
ID HIS81_BACAN Reviewed; 370 AA.
AC Q81SV5; Q6I134; Q6KUY8;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Histidinol-phosphate aminotransferase 1;
DE EC=2.6.1.9;
DE AltName: Full=Imidazole acetol-phosphate transaminase 1;
GN Name=hisC1; Synonyms=hisC-1; OrderedLocusNames=BA_1539, GBAA_1539, BAS1428;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC ChEBI:CHEBI:57980; EC=2.6.1.9;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000305}.
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DR EMBL; AE016879; AAP25476.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT30637.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53748.1; -; Genomic_DNA.
DR RefSeq; NP_843990.1; NC_003997.3.
DR RefSeq; WP_001264013.1; NZ_WXXJ01000001.1.
DR RefSeq; YP_027697.1; NC_005945.1.
DR AlphaFoldDB; Q81SV5; -.
DR SMR; Q81SV5; -.
DR STRING; 261594.GBAA_1539; -.
DR DNASU; 1087402; -.
DR EnsemblBacteria; AAP25476; AAP25476; BA_1539.
DR EnsemblBacteria; AAT30637; AAT30637; GBAA_1539.
DR GeneID; 45021513; -.
DR KEGG; ban:BA_1539; -.
DR KEGG; bar:GBAA_1539; -.
DR KEGG; bat:BAS1428; -.
DR PATRIC; fig|198094.11.peg.1511; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_9; -.
DR OMA; IWLNANE; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..370
FT /note="Histidinol-phosphate aminotransferase 1"
FT /id="PRO_0000153297"
FT MOD_RES 222
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 370 AA; 41602 MW; 8B0C1F6DAD14851B CRC64;
MRVKEQLLTL RAYVPGKNIE EVKREYGLSK IVKLASNENP FGCSARVTEA LTSLASQYAL
YPDGHAFELR TQVAKHLGVK AEQLLFGSGL DEVIQMISRA LLHEGTNVVM ANPTFSQYHH
HAVIEGAEVR EVSLKDGIHD LDAMLQQVDD QTKIVWICNP NNPTGTYVEK QKLLSFLESV
PKSALVIMDE AYYEYAGAED YPQTLPLLEK YENLMVLRTF SKAYGLAAFR IGYAVGNTEL
IGQLEVARLP FNTSTVAQSV ALAALEDQAF LQECVKKNEE GLHQYYAFCK EYNVFYYPSQ
TNFIFLKLGI PGNEAFERLM KKGYIVRSGA AFGIDDGIRI TVGLKEENDE IIELLKELVN
EQVQKEETYS