HIS4_BRUA2
ID HIS4_BRUA2 Reviewed; 243 AA.
AC Q2YQY9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=BAB1_2085;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(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; AM040264; CAJ12041.1; -; Genomic_DNA.
DR RefSeq; WP_002965150.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YQY9; -.
DR SMR; Q2YQY9; -.
DR STRING; 359391.BAB1_2085; -.
DR EnsemblBacteria; CAJ12041; CAJ12041; BAB1_2085.
DR GeneID; 45125338; -.
DR GeneID; 55591654; -.
DR KEGG; bmf:BAB1_2085; -.
DR PATRIC; fig|359391.11.peg.1319; -.
DR HOGENOM; CLU_048577_1_1_5; -.
DR OMA; EWLHLVD; -.
DR PhylomeDB; Q2YQY9; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000002719; Chromosome I.
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..243
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_0000229045"
FT ACT_SITE 8
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
SQ SEQUENCE 243 AA; 25589 MW; 1B264AC48A4D199A CRC64;
MILFPAIDLK DGQCVRLKLG DMDQATIYNE DPAAQAKAFE DQGFEWLHVV DLNGAFAGES
VNGTAVEAIL KATKNPVQLG GGIRTLAHIE NWLSRGLRRV ILGTVAVRDP ALVMEACKAF
PGQVAVGIDA KGGKVAVEGW AEASRLGVIE LAKKFEGAGV AAIIYTDIDR DGVLAGINWD
STLALAEAVS IPVIASGGLA SMEDIRRLAT PEMRKLEGAI SGRALYDGRI DPAEALSVLR
AAA