HIS4_XANOR
ID HIS4_XANOR Reviewed; 244 AA.
AC Q5H0K7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000255|HAMAP-Rule:MF_01014};
DE EC=5.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01014};
DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000255|HAMAP-Rule:MF_01014};
GN Name=hisA {ECO:0000255|HAMAP-Rule:MF_01014}; OrderedLocusNames=XOO2260;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-
CC phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469,
CC ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01014};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC {ECO:0000255|HAMAP-Rule:MF_01014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01014}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP-
CC Rule:MF_01014}.
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DR EMBL; AE013598; AAW75514.1; -; Genomic_DNA.
DR RefSeq; WP_011258946.1; NC_006834.1.
DR AlphaFoldDB; Q5H0K7; -.
DR SMR; Q5H0K7; -.
DR STRING; 291331.XOO2260; -.
DR EnsemblBacteria; AAW75514; AAW75514; XOO2260.
DR KEGG; xoo:XOO2260; -.
DR HOGENOM; CLU_048577_1_2_6; -.
DR OMA; EWLHLVD; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000006735; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04732; HisA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01014; HisA; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR006063; HisA_bact_arch.
DR InterPro; IPR044524; Isoase_HisA-like.
DR InterPro; IPR023016; Isoase_HisA-like_bact.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR43090; PTHR43090; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00007; TIGR00007; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Isomerase;
KW Reference proteome.
FT CHAIN 1..244
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_0000229096"
FT ACT_SITE 10
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT ACT_SITE 132
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
SQ SEQUENCE 244 AA; 25758 MW; AA7F9946C5CE327F CRC64;
MSFTVYPALD IRNGRVVRLL QGDYARETHY GNDVLPRAQA FADAGAQWMH LVDLDAAKAG
GYTLATTLGE IARATGLQVQ TGGGVRSRDD VASILDAGAA RVVIGSLAVR DSEMVIAWLQ
EFGADRLTIA LDTRQDTDGI WQLPVHGWTE TADATLDQLA VRYAQAGLKH LLCTDIARDG
MLSGPNAALY AHLRSLTPQL QVQVSGGARN LADVAAAKAA GCAGIVLGKA LLEGHLDLDE
ALAC