ID   HIS4_NITV2              Reviewed;         249 AA.
AC   P62353;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   28-JAN-2026, entry version 114.
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};
GN   OrderedLocusNames=DVU_1038;
OS   Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 /
OS   NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC   Desulfovibrionales; Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 /
RC   Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017285; AAS95518.1; -; Genomic_DNA.
DR   RefSeq; WP_010938337.1; NC_002937.3.
DR   AlphaFoldDB; P62353; -.
DR   SMR; P62353; -.
DR   STRING; 882.DVU_1038; -.
DR   PaxDb; 882-DVU_1038; -.
DR   EnsemblBacteria; AAS95518; AAS95518; DVU_1038.
DR   KEGG; dvu:DVU_1038; -.
DR   PATRIC; fig|882.5.peg.976; -.
DR   eggNOG; COG0106; Bacteria.
DR   HOGENOM; CLU_048577_1_1_7; -.
DR   OrthoDB; 9807749at2; -.
DR   PhylomeDB; P62353; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000002194; 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:L-histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:L-tryptophan biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd04732; HisA; 1.
DR   FunFam; 3.20.20.70:FF:000009; 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; 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; IPR023016; HisA/PriA.
DR   InterPro; IPR006063; HisA_bact_arch.
DR   InterPro; IPR044524; Isoase_HisA-like.
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..249
FT                   /note="1-(5-phosphoribosyl)-5-[(5-
FT                   phosphoribosylamino)methylideneamino] imidazole-4-
FT                   carboxamide isomerase"
FT                   /id="PRO_0000142003"
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   249 AA;  26540 MW;  71C5EE681860F858 CRC64;
     MIVFPAIDLM NGVCVRLRRG RADDETVFSS DPVATARHWQ EQGGRWLHVV DLDGAFSGQP
     VNAPLIRSIC DALDIPVQLG GGIRDAATAK AYLEAGVERL IIGTIALEEP DAYAALCAEF
     PGRIGVSLDA EGGKLKTKGW VADSGLTVDE VLPRLLEAGT AFIIYTDIDR DGMQTGVNLP
     ALEHLAKAST VPVIAAGGVA TLEDVKALYP LSRTTNLQGA VSGRAIYEGT LDLRTAMDWI
     RQQEKAEAC
//