ID   HIS4_RHOCB              Reviewed;         239 AA.
AC   O30725; D5ARP1;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   27-MAR-2024, entry version 120.
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=RCAP_rcc01154;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MT1131;
RX   PubMed=9473054; DOI=10.1128/jb.180.4.969-978.1998;
RA   Koch H.G., Hwang O., Daldal F.;
RT   "Isolation and characterization of Rhodobacter capsulatus mutants affected
RT   in cytochrome cbb3 oxidase activity.";
RL   J. Bacteriol. 180:969-978(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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}.
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; AF016223; AAC46106.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE84912.1; -; Genomic_DNA.
DR   RefSeq; WP_013066891.1; NC_014034.1.
DR   AlphaFoldDB; O30725; -.
DR   SMR; O30725; -.
DR   STRING; 272942.RCAP_rcc01154; -.
DR   GeneID; 31490067; -.
DR   KEGG; rcp:RCAP_rcc01154; -.
DR   eggNOG; COG0106; Bacteria.
DR   HOGENOM; CLU_048577_1_1_5; -.
DR   OrthoDB; 9807749at2; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000002361; 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; 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..239
FT                   /note="1-(5-phosphoribosyl)-5-[(5-
FT                   phosphoribosylamino)methylideneamino] imidazole-4-
FT                   carboxamide isomerase"
FT                   /id="PRO_0000142044"
FT   ACT_SITE        8
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        210
FT                   /note="D -> N (in Ref. 1; AAC46106)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="I -> F (in Ref. 1; AAC46106)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223..225
FT                   /note="IYD -> LYN (in Ref. 1; AAC46106)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="D -> N (in Ref. 1; AAC46106)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235..239
FT                   /note="AALKA -> RP (in Ref. 1; AAC46106)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   239 AA;  24468 MW;  E5ACBE5A88A1ABCC CRC64;
     MILYPAIDLK DGNCVRLLHG EMDKATVFGT DPAAQAAKFE AAGCAWVHLV DLNGAFAGEP
     VNGAAVEAIL ARITVPAQLG GGIRDMATIE RWLSKGLARV ILGTVAVENP DLVREAAKAF
     PGQVAVGIDA RNGKVATKGW ATETDVLVTD LAQSFEDAGV AAIIYTDILR DGAMTGPNIE
     ATEALGRAVT IPVIASGGVS SLPDLIALRD TGVIAGAISG RAIYDGALDL QAALAALKA
//