HIS8_RHOCS
ID HIS8_RHOCS Reviewed; 362 AA.
AC B6IYQ0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Histidinol-phosphate aminotransferase {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 {ECO:0000255|HAMAP-Rule:MF_01023};
GN Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=RC1_4085;
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW;
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) 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; 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; CP000613; ACJ01424.1; -; Genomic_DNA.
DR RefSeq; WP_012569197.1; NC_011420.2.
DR AlphaFoldDB; B6IYQ0; -.
DR SMR; B6IYQ0; -.
DR STRING; 414684.RC1_4085; -.
DR EnsemblBacteria; ACJ01424; ACJ01424; RC1_4085.
DR KEGG; rce:RC1_4085; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_5; -.
DR OMA; YPDMACT; -.
DR OrthoDB; 1248286at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000001591; 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..362
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_1000135414"
FT MOD_RES 220
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 362 AA; 38554 MW; 8BC0F7D31DACBFB5 CRC64;
MSGPIPNPGI LDIAPYVGGE HSAPGVTRLL RLASNEGALG PSPRAVEAFR AVGPEIHRYP
DGGSTRLREA IGHRFGLDPA RVLCFNGSDE VLHLLAQAYA GPGGEVLYSR HGFLVYPIAA
RAAGATPVAA PERNLTTDVD ALLARVSERT RIVYVANPNN PTGSYLPADA LARLHAGLPP
HVLLVIDAAY AEYVTANDYA DGTALVARFD NVVMTRTFSK LFGLGGMRLG WAYCPPAVAD
ALHRVRSPFN VSVAAQAAGV AALEDLEFQE RSRALNEQSR TAFTGRVRAL GLVVHPSVCN
FVLVDFAATG RPAEEARQFL KARGILVRQM GAYGLPDCLR ITMGLPAEME EVADALGDWL
KG