HIS4_BRAHW
ID HIS4_BRAHW Reviewed; 238 AA.
AC C0QWR6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=BHWA1_02263;
OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX NCBI_TaxID=565034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49526 / WA1;
RX PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA Barrero R., Phillips N.D., Hampson D.J.;
RT "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT intestine.";
RL PLoS ONE 4:E4641-E4641(2009).
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; CP001357; ACN84719.1; -; Genomic_DNA.
DR RefSeq; WP_012671751.1; NC_012225.1.
DR AlphaFoldDB; C0QWR6; -.
DR SMR; C0QWR6; -.
DR STRING; 565034.BHWA1_02263; -.
DR EnsemblBacteria; ACN84719; ACN84719; BHWA1_02263.
DR KEGG; bhy:BHWA1_02263; -.
DR eggNOG; COG0106; Bacteria.
DR HOGENOM; CLU_048577_1_2_12; -.
DR OMA; EWLHLVD; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000001803; 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.
FT CHAIN 1..238
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_1000148955"
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 238 AA; 26749 MW; BC2F086D054696BC CRC64;
MYILPAIDLK NGEVVRLVEG NYDNKTTYFK DPLEVLDFFI ESGSSYLHVV DLDGASDGET
INFKTIEKVI KKCDLFVEVG GGIRNEDTIK KYLDIGVKRT ILGTAAVENI DFTNNMINKY
KEHIAVSIDS RDRMIAVKGW KEINKQDSVE FCMKLDSMGI DTIIYTDISK DGKLSGTNLD
IYKELREKIS CNIIASGGVT FEDEIIKLRD MKINGAIVGK AIYEGKIDLK KIIEIAKQ