ID   HIS81_DECAR             Reviewed;         362 AA.
AC   Q47GP2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   02-SEP-2026, entry version 105.
DE   RecName: Full=Histidinol-phosphate aminotransferase 1 {ECO:0000255|HAMAP-Rule:MF_01023};
DE            EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023};
DE   AltName: Full=Imidazole acetol-phosphate transaminase 1 {ECO:0000255|HAMAP-Rule:MF_01023};
GN   Name=hisC1 {ECO:0000255|HAMAP-Rule:MF_01023};
GN   OrderedLocusNames=Daro_1233;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Rhodocyclales; Azonexaceae; Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidinol phosphate + 2-oxoglutarate = 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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01023};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01023};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01023}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
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DR   EMBL; CP000089; AAZ45989.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47GP2; -.
DR   SMR; Q47GP2; -.
DR   STRING; 159087.Daro_1233; -.
DR   KEGG; dar:Daro_1233; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_4; -.
DR   OrthoDB; 9813612at2; -.
DR   UniPathway; UPA00031; UER00012.
DR   GO; GO:0004400; F:L-histidinol-phosphate:2-oxoglutarate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:L-histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR050106; HistidinolP_aminotransfase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01141; hisC; 1.
DR   PANTHER; PTHR43643:SF3; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43643; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..362
FT                   /note="Histidinol-phosphate aminotransferase 1"
FT                   /id="PRO_0000153352"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   362 AA;  39502 MW;  CF3EBA40D23D7D31 CRC64;
     MSLADQALSY VRAISPYQPG KPITELAREM GIPVEKIVKL ASNENPLGMS PKARKAVEAA
     ISGIERYPDQ FDLIAKVAER CGVSSNQIVL GNGSNDVLDL IARVFLAPGR SAVFAQHAFA
     VYPLATLSTG AELISTPAKN YGHDLNAMRA AIRPDTRIVW IANPNNPTGN FLPYPEVRAF
     LEVVPKDVVV VLDEAYNEYI PPAERVDTAT WIKDFPNLVV CRTFSKIFGL AGLRVGYALA
     STEVADLMNR IRQPFNVNNL AIAAAVAALD DHLFVADSYE LNRRGMEQII AGLKRFGLEH
     IPSHGNFVTF RAGDAAVVNQ KLLKQGVIVR PIGGYGLPEW LRVTIGTEPE NARFLEALEK
     AL
//