ID   HIS8_MYCTO              Reviewed;         380 AA.
AC   P9WML6; L0T9Y3; O06591; P0A678;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisC; Synonyms=hisC1; OrderedLocusNames=MT1636;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK45904.1; -; Genomic_DNA.
DR   PIR; B70544; B70544.
DR   RefSeq; WP_003407947.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WML6; -.
DR   SMR; P9WML6; -.
DR   EnsemblBacteria; AAK45904; AAK45904; MT1636.
DR   KEGG; mtc:MT1636; -.
DR   PATRIC; fig|83331.31.peg.1758; -.
DR   HOGENOM; CLU_017584_3_1_11; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001020; 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; Transferase.
FT   CHAIN           1..380
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000427282"
FT   MOD_RES         232
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  40581 MW;  490B2865E361587A CRC64;
     MTRSGHPVTL DDLPLRADLR GKAPYGAPQL AVPVRLNTNE NPHPPTRALV DDVVRSVREA
     AIDLHRYPDR DAVALRADLA GYLTAQTGIQ LGVENIWAAN GSNEILQQLL QAFGGPGRSA
     IGFVPSYSMH PIISDGTHTE WIEASRANDF GLDVDVAVAA VVDRKPDVVF IASPNNPSGQ
     SVSLPDLCKL LDVAPGIAIV DEAYGEFSSQ PSAVSLVEEY PSKLVVTRTM SKAFAFAGGR
     LGYLIATPAV IDAMLLVRLP YHLSSVTQAA ARAALRHSDD TLSSVAALIA ERERVTTSLN
     DMGFRVIPSD ANFVLFGEFA DAPAAWRRYL EAGILIRDVG IPGYLRATTG LAEENDAFLR
     ASARIATDLV PVTRSPVGAP