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Database: UniProt
Entry: A0A0G1GVH5_9BACT
LinkDB: A0A0G1GVH5_9BACT
Original site: A0A0G1GVH5_9BACT 
ID   A0A0G1GVH5_9BACT        Unreviewed;       238 AA.
AC   A0A0G1GVH5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino) methylideneamino] imidazole-4-carboxamide isomerase, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000313|EMBL:KKT02634.1};
DE            EC=5.3.1.16 {ECO:0000313|EMBL:KKT02634.1};
GN   ORFNames=UV80_C0002G0101 {ECO:0000313|EMBL:KKT02634.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWF2_43_17.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619068 {ECO:0000313|EMBL:KKT02634.1, ECO:0000313|Proteomes:UP000034674};
RN   [1] {ECO:0000313|EMBL:KKT02634.1, ECO:0000313|Proteomes:UP000034674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:KKT02634.1}.
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DR   EMBL; LCFW01000002; KKT02634.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1GVH5; -.
DR   STRING; 1619068.UV80_C0002G0101; -.
DR   Proteomes; UP000034674; 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-KW.
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; 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}; Isomerase {ECO:0000313|EMBL:KKT02634.1}.
SQ   SEQUENCE   238 AA;  26337 MW;  B7E7221B9C581924 CRC64;
     MQVIPCFYIQ DGKCVSLYKG QQNKQKKIYF TEPLQMARLF DMQGAKKLQI IDLNGSITGE
     LGNARLIQKI CKDIKSEVQL GGGIRKIGDM EKAFELGASR VVLGVSSIAI LKSALKKYGG
     EKIIMGIKAR HNIVDTDLML EGKIPEVTLL AKEVKEIGVT QIIYKDLEAE GTLYHPNFDM
     IEKIIYETGG EVDVYSSGGV ADAYDLKLLK DTGAAGVIIN RAFMENELSF PDLNNIFH
//
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