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Database: UniProt
Entry: A0A0R2Q0U5_9ACTN
LinkDB: A0A0R2Q0U5_9ACTN
Original site: A0A0R2Q0U5_9ACTN 
ID   A0A0R2Q0U5_9ACTN        Unreviewed;       226 AA.
AC   A0A0R2Q0U5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamideisomerase {ECO:0000256|ARBA:ARBA00012550};
DE            EC=5.3.1.16 {ECO:0000256|ARBA:ARBA00012550};
GN   ORFNames=ABR67_02730 {ECO:0000313|EMBL:KRO43833.1};
OS   Acidimicrobium sp. BACL17 MAG-120823-bin42.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Acidimicrobiaceae; Acidimicrobium.
OX   NCBI_TaxID=1655575 {ECO:0000313|EMBL:KRO43833.1, ECO:0000313|Proteomes:UP000051003};
RN   [1] {ECO:0000313|EMBL:KRO43833.1, ECO:0000313|Proteomes:UP000051003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL27 MAG-120823-bin42 {ECO:0000313|EMBL:KRO43833.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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};
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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family.
CC       {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|RuleBase:RU003657}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRO43833.1}.
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DR   EMBL; LIAZ01000024; KRO43833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2Q0U5; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000051003; Unassembled WGS sequence.
DR   GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04732; HisA; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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,
KW   ECO:0000256|RuleBase:RU003657};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW   ECO:0000256|RuleBase:RU003657};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KRO43833.1}.
SQ   SEQUENCE   226 AA;  24093 MW;  CC085428CE39D4BA CRC64;
     MVVPCIDIQD GQVVQLVQGR ERALVGPDPL EMLELFAGFP EIQIIDLDAA MGVGENFEII
     EMLASKATCR VGGGVRSAQR ARQLIDLGAH RVIVGTAAFT DAFDGIVQEV SSRNILVALD
     SKAGKVVVDG WNTMLHTTAI EAVSGFTEMC SGFLCTYVDK EGMMQGTDLE WFAQLRSATS
     LSITAAGGIT TLDDVRSLLA MNIDAAIGMA VYTGSLSLDD LVMLMQ
//
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