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Database: UniProt
Entry: A0A0S4Q549_BLAVI
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ID   A0A0S4Q549_BLAVI        Unreviewed;       224 AA.
AC   A0A0S4Q549;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000256|HAMAP-Rule:MF_01014};
DE            EC=5.3.1.16 {ECO:0000256|HAMAP-Rule:MF_01014};
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000256|HAMAP-Rule:MF_01014};
GN   Name=hisA_1 {ECO:0000313|EMBL:CUU43690.1};
GN   Synonyms=hisA {ECO:0000256|HAMAP-Rule:MF_01014};
GN   ORFNames=BVIRIDIS_27160 {ECO:0000313|EMBL:CUU43690.1};
OS   Blastochloris viridis (Rhodopseudomonas viridis).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Blastochloridaceae; Blastochloris.
OX   NCBI_TaxID=1079 {ECO:0000313|EMBL:CUU43690.1, ECO:0000313|Proteomes:UP000065734};
RN   [1] {ECO:0000313|Proteomes:UP000065734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19567 / DSM 133 / F {ECO:0000313|Proteomes:UP000065734};
RX   PubMed=26798090; DOI=10.1128/genomeA.01520-15;
RA   Liu L.N., Faulkner M., Liu X., Huang F., Darby A.C., Hall N.;
RT   "Revised genome sequence of the purple photosynthetic bacterium
RT   Blastochloris viridis.";
RL   Genome Announc. 4:0-0(2016).
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:0000256|ARBA:ARBA00000901, ECO:0000256|HAMAP-
CC         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:0000256|ARBA:ARBA00005133, ECO:0000256|HAMAP-Rule:MF_01014}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01014}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family.
CC       {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|HAMAP-Rule:MF_01014,
CC       ECO:0000256|RuleBase:RU003657}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01014}.
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DR   EMBL; LN907867; CUU43690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4Q549; -.
DR   STRING; 1079.BVIR_3272; -.
DR   PATRIC; fig|1079.7.peg.2872; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000065734; 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; Aldolase class I; 1.
DR   HAMAP; MF_01014; HisA; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR044524; Isoase_HisA-like.
DR   InterPro; IPR023016; Isoase_HisA-like_bact.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01014}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01014};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01014};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065734}.
FT   ACT_SITE        108
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01014"
SQ   SEQUENCE   224 AA;  22671 MW;  395F3D7B80DB9342 CRC64;
     MARATVFNAD PAAQARAFAG AGFSWLHVVD LDGAFAGRPI NASAVGTILE NVSIPVQLGG
     GIRNMATIES WLKRGVARVV IGTAAIKDPA LVREAARAFP GQIAVGLDAK DGFIAVEGWA
     EDSDATVLDT AKRFEDAGVA AIIYTDIGRD GLLKGLNVGA TAALARAISI PVIASGGLAS
     LDDVRRLLSD EGAGITGAIA GRALYDGRLD PAEALALVAV AAAA
//
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