ID   HIS4_VIBCH              Reviewed;         245 AA.
AC   Q9KSW9;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase;
DE            EC=5.3.1.16;
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase;
GN   Name=hisA; OrderedLocusNames=VC_1137;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR   EMBL; AE003852; AAF94296.1; -; Genomic_DNA.
DR   PIR; D82238; D82238.
DR   RefSeq; NP_230782.1; NC_002505.1.
DR   RefSeq; WP_000586511.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KSW9; -.
DR   SMR; Q9KSW9; -.
DR   STRING; 243277.VC_1137; -.
DR   DNASU; 2614407; -.
DR   EnsemblBacteria; AAF94296; AAF94296; VC_1137.
DR   KEGG; vch:VC_1137; -.
DR   PATRIC; fig|243277.26.peg.1086; -.
DR   eggNOG; COG0106; Bacteria.
DR   HOGENOM; CLU_048577_1_2_6; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IBA:GO_Central.
DR   GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR   CDD; cd04732; HisA; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR00007; 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase; 1.
DR   PANTHER; PTHR43090; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   PANTHER; PTHR43090:SF2; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Isomerase;
KW   Reference proteome.
FT   CHAIN           1..245
FT                   /note="1-(5-phosphoribosyl)-5-[(5-
FT                   phosphoribosylamino)methylideneamino] imidazole-4-
FT                   carboxamide isomerase"
FT                   /id="PRO_0000142071"
FT   ACT_SITE        7
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   245 AA;  26339 MW;  5A913A5ABEC55D3D CRC64;
     MIIPALDLIE GQVVRLYQGD YGQVTEYKVD PAEQFNLYHQ AGAGWLHLVD LTGAKNTAAR
     QLNLIARLLA STPANIQIGG GVRSEQDVVD LLEAGAQRVV VGSTAVKQPQ LVKSWIEKYG
     AEKIVLALDI NIDEQGTRKV AISGWQEDSG VTIEALIDDY LTVGLQHVLC TDISRDGTLA
     GSNVELYRDL CRQYPQVQFQ SSGGIGSLAD IEALKGTGVA GVIVGRALLD GKFTAQEAFA
     CWQNG
//