ID A0A1I3LKU1_9GAMM Unreviewed; 348 AA. AC A0A1I3LKU1; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 22-FEB-2023, entry version 11. DE RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_01023}; DE EC=2.6.1.9 {ECO:0000256|HAMAP-Rule:MF_01023}; DE AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000256|HAMAP-Rule:MF_01023}; GN Name=hisC {ECO:0000256|HAMAP-Rule:MF_01023}; GN ORFNames=SAMN05216194_101643 {ECO:0000313|EMBL:SFI85313.1}; OS Stutzerimonas kunmingensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Stutzerimonas. OX NCBI_TaxID=1211807 {ECO:0000313|EMBL:SFI85313.1, ECO:0000313|Proteomes:UP000242255}; RN [1] {ECO:0000313|EMBL:SFI85313.1, ECO:0000313|Proteomes:UP000242255} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 25974 {ECO:0000313|EMBL:SFI85313.1, RC ECO:0000313|Proteomes:UP000242255}; RA de Groot N.N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. 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 Evidence={ECO:0000256|ARBA:ARBA00001045, ECO:0000256|HAMAP- CC Rule:MF_01023}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|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:0000256|ARBA:ARBA00005011, ECO:0000256|HAMAP-Rule:MF_01023}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_01023}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. Histidinol-phosphate aminotransferase CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01023}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FORS01000001; SFI85313.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1I3LKU1; -. DR EnsemblBacteria; SFI85313; SFI85313; SAMN05216194_101643. DR UniPathway; UPA00031; UER00012. DR Proteomes; UP000242255; Unassembled WGS sequence. 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 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; 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 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. DR TIGRFAMs; TIGR01141; hisC; 1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023}; KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP- KW Rule:MF_01023}; Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01023}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000313|EMBL:SFI85313.1}. FT DOMAIN 25..347 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" FT MOD_RES 210 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01023" SQ SEQUENCE 348 AA; 38331 MW; 1B2EE221ED191EB4 CRC64; MSKFWSPFVK DLVPYVPGEQ PKLSKLVKLN TNENPYGPSP RAIAAMQAEL NDGLRLYPDP NGERLKHAVA EYYGVCPAQV FVGNGSDEVL AHAFHGLFQH DRPLLFPDIS YSFYPVYCGL YGIAYETVAL DEQFQIDVAD YNRPNGGIIF PNPNAPTGCL LPLQAIEQLL QANTESVVLV DEAYVDFGGE SAIALVDRYP NLLVTQTLSK SRSLAGLRVG LAVGHPDLIE ALERIKNSFN SYPLDRIAIA GAAAAFEDRA HFQQTCQQVI DSREAVVTAM QRLGFEVLPS AANFIFARHP QRDAAEVAAS LREQGVIVRH FKQPRIEQFL RITIGTPEQN HALLAALG //