ID   HIS8_BACSU              Reviewed;         360 AA.
AC   P17731; O32008; Q45651;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisC; Synonyms=hisH; OrderedLocusNames=BSU22620;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3106153; DOI=10.1016/0378-1119(86)90394-x;
RA   Henner D.J., Band L., Flaggs G., Chen E.;
RT   "The organization and nucleotide sequence of the Bacillus subtilis hisH,
RT   tyrA and aroE genes.";
RL   Gene 49:147-152(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 267.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-110.
RC   STRAIN=168;
RX   PubMed=3924737; DOI=10.1016/0378-1119(85)90125-8;
RA   Henner D.J., Band L., Shimotsu H.;
RT   "Nucleotide sequence of the Bacillus subtilis tryptophan operon.";
RL   Gene 34:169-177(1985).
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; M80245; AAA20867.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14178.2; -; Genomic_DNA.
DR   EMBL; K01391; AAA22871.1; -; Genomic_DNA.
DR   PIR; A26532; A26532.
DR   RefSeq; NP_390143.2; NC_000964.3.
DR   RefSeq; WP_004399129.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P17731; -.
DR   SMR; P17731; -.
DR   IntAct; P17731; 1.
DR   MINT; P17731; -.
DR   STRING; 224308.BSU22620; -.
DR   jPOST; P17731; -.
DR   PaxDb; P17731; -.
DR   PRIDE; P17731; -.
DR   EnsemblBacteria; CAB14178; CAB14178; BSU_22620.
DR   GeneID; 939009; -.
DR   KEGG; bsu:BSU22620; -.
DR   eggNOG; COG0079; Bacteria.
DR   InParanoid; P17731; -.
DR   OMA; IWLNANE; -.
DR   PhylomeDB; P17731; -.
DR   BioCyc; BSUB:BSU22620-MON; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001570; 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..360
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153308"
FT   MOD_RES         223
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        43..57
FT                   /note="CSEAAKEALHHEIQQ -> LLQRLQKRRFIMIQH (in Ref. 3;
FT                   AAA22871)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63..71
FT                   /note="DGYSAALRT -> EVLAPFGP (in Ref. 3; AAA22871)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="L -> H (in Ref. 3; AAA22871)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        267
FT                   /note="D -> Y (in Ref. 1; AAA20867)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  40036 MW;  49F5CB32C45FF979 CRC64;
     MRIKEHLKQL KPYQPGKPIE AVKSEYGLDK VVKLASNENP YGCSEAAKEA LHHEIQQLAL
     YPDGYSAALR TRLSKHLNVS ETSLIFGNGS DEIIQIICRA FLNDKTNTVT AAPTFPQYKH
     NAVIEGAEVR EIALRPDGSH DLDAMLEAID EQTQVVWICS PNNPTGTYTS EGELLAFLER
     VPSRVLVVLD EAYYEYVTAE DYPETVPLLS KYSNLMILRT FSKAYGLAAL RVGYGIADEN
     LIRQIEPARE PFNTSRLGQA AAIAALDDQA FIASCVEQNN AGLQQYYDFA KTHGLKCYPS
     QTNFVLIDFK RPADELFQAL LEKGYIVRSG NALGFPTSLR ITIGTKEQNE EILAILAEIL