ID   HIS8_SINFN              Reviewed;         368 AA.
AC   P55683;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisC; OrderedLocusNames=NGR_a01000; ORFNames=y4wE;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; U00090; AAB91912.1; -; Genomic_DNA.
DR   RefSeq; NP_444125.1; NC_000914.2.
DR   AlphaFoldDB; P55683; -.
DR   SMR; P55683; -.
DR   STRING; 394.NGR_a01000; -.
DR   EnsemblBacteria; AAB91912; AAB91912; NGR_a01000.
DR   KEGG; rhi:NGR_a01000; -.
DR   PATRIC; fig|394.7.peg.86; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_0_5; -.
DR   OMA; IWLNANE; -.
DR   OrthoDB; 1248286at2; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
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; Plasmid;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..368
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153438"
FT   MOD_RES         223
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   368 AA;  40421 MW;  92127E5CF0884896 CRC64;
     MERTMSDAKL QRVLSSLTEV YRQLNSLPSS QPSDAGYVKL DTNENPFALP KAVMQSAVAA
     LERQYLYPED DNISLREAAA ASYDLSADQV IAGNGSSELL SLIYKAFLGP GDSVAMLSPG
     FAYNRKLAQL QGARLLEIKW GESSLLPIHE LLFGPAKQAK FILLANPNNP TGTFVPIADI
     ESLVALSDQL VVLDEAYVDF APDSALRLVN RYSNLLLLRT FSKSYAAAGI RVGFGFGHPE
     VIGRLRNIQN MFNMNVIGHA VGVSILAHRA TYNENHRHIR HERERVRVAL SRLGFSVTPS
     HANFLLARVP AGRDGVWWHA CLKRKKILVA VLPDEGLEDC IRVSIGTKPQ MDAFLAAVED
     ISGAQQSR