ID   HIS81_CAUVC             Reviewed;         359 AA.
AC   Q9A671;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Histidinol-phosphate aminotransferase 1;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase 1;
GN   Name=hisC1; OrderedLocusNames=CC_2223;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK24194.1; -; Genomic_DNA.
DR   PIR; F87524; F87524.
DR   RefSeq; NP_421026.1; NC_002696.2.
DR   AlphaFoldDB; Q9A671; -.
DR   SMR; Q9A671; -.
DR   STRING; 190650.CC_2223; -.
DR   EnsemblBacteria; AAK24194; AAK24194; CC_2223.
DR   KEGG; ccr:CC_2223; -.
DR   PATRIC; fig|190650.5.peg.2240; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_5; -.
DR   OMA; YPDMACT; -.
DR   BioCyc; CAULO:CC2223-MON; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001816; 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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..359
FT                   /note="Histidinol-phosphate aminotransferase 1"
FT                   /id="PRO_0000153342"
FT   MOD_RES         216
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   359 AA;  39262 MW;  A2EFE47EDA0B6C65 CRC64;
     MPKPGIMDIH AYVGGKSKVE GIAHPVKLSS NENILGSSDK AKDAYRNAVD RLHIYPDGKA
     NFLRAAVAER YKLEPERLTF GDGSDEIFAL LCQVYLEPGD NIVQGEHGFA AYAIGARACQ
     GEVRMAKEVN HRVDIDEVIK CVDERTRLVF IANPANPTGT WLTGEEIRAL HAALPPSVVL
     VLDGAYAEFC SDPHFEDGLE LARTAENVIV TRTFSKIHGL AALRVGWGYA PEHIIAPIER
     IRPPFNTSIP AQEAAVAALF DDDFQDRSRA LVEQWRPWLA QQLGGLGLEV TPSAANFVLA
     TFPTTPGKTA PEAEAFLASK GYLVRAVGNY NLPHAIRITI GLEEQNRAVV ELLSQFMGR