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Database: UniProt
Entry: A0A401U8J9_9BACT
LinkDB: A0A401U8J9_9BACT
Original site: A0A401U8J9_9BACT 
ID   A0A401U8J9_9BACT        Unreviewed;       230 AA.
AC   A0A401U8J9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
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=SanaruYs_14330 {ECO:0000313|EMBL:GCC51213.1};
OS   Chryseotalea sanaruensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Chryseotalea.
OX   NCBI_TaxID=2482724 {ECO:0000313|EMBL:GCC51213.1, ECO:0000313|Proteomes:UP000288227};
RN   [1] {ECO:0000313|EMBL:GCC51213.1, ECO:0000313|Proteomes:UP000288227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ys {ECO:0000313|EMBL:GCC51213.1,
RC   ECO:0000313|Proteomes:UP000288227};
RA   Maejima Y., Iino T., Muraguchi Y., Fukuda K., Ohkuma M., Moriuchi R.,
RA   Dohra H., Kimbara K., Shintani M.;
RT   "Chryseotalea sanarue gen. nov., sp., nov., a member of the family
RT   Cytophagaceae, isolated from a brackish lake in Hamamatsu Japan.";
RL   Submitted (NOV-2018) 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:GCC51213.1}.
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DR   EMBL; BHXQ01000002; GCC51213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401U8J9; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000288227; 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:GCC51213.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288227}.
SQ   SEQUENCE   230 AA;  25460 MW;  CBE322A4D71DA487 CRC64;
     MRKGDPLSEK AYDENPLDLA KRFEDHGIEV VHLVDLEGAE KGSPKNFHVV EAIAGYTDLK
     IDFTGGISTD GDIAKAYEAG AHYITASSIA VTDPDLFASW VVTYGREKIT LGADVTDIVS
     KEIAFRGWQK KAHKGLVEHV KFFYDRGLKY VKTTDISRDG VLEGPAFDFY ADMIKTFPEI
     SVLASGGVRG VDDIQRLNDI GVFAVIFGKA YYEGILKLKD LERFLTKKEA
//
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