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Database: UniProt
Entry: A0A0N1H685_9EURO
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ID   A0A0N1H685_9EURO        Unreviewed;       257 AA.
AC   A0A0N1H685;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000256|ARBA:ARBA00018464, ECO:0000256|RuleBase:RU364022};
DE            EC=5.3.1.16 {ECO:0000256|ARBA:ARBA00012550, ECO:0000256|RuleBase:RU364022};
DE   AltName: Full=5-proFAR isomerase {ECO:0000256|ARBA:ARBA00031376, ECO:0000256|RuleBase:RU364022};
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000256|ARBA:ARBA00030547, ECO:0000256|RuleBase:RU364022};
GN   ORFNames=AB675_9332 {ECO:0000313|EMBL:KPI41484.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI41484.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI41484.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI41484.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-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|RuleBase:RU364022};
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|RuleBase:RU364022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364022}.
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:KPI41484.1}.
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DR   EMBL; LFJN01000009; KPI41484.1; -; Genomic_DNA.
DR   RefSeq; XP_018001447.1; XM_018149856.1.
DR   AlphaFoldDB; A0A0N1H685; -.
DR   STRING; 1664694.A0A0N1H685; -.
DR   GeneID; 28741736; -.
DR   OrthoDB; 312953at2759; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000038010; Unassembled WGS sequence.
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-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04723; HisA_HisF; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011858; His6-like_euk.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR044524; Isoase_HisA-like.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR02129; hisA_euk; 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 {ECO:0000256|RuleBase:RU003657};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364022};
KW   Histidine biosynthesis {ECO:0000256|RuleBase:RU003657};
KW   Isomerase {ECO:0000256|RuleBase:RU364022, ECO:0000313|EMBL:KPI41484.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000038010}.
SQ   SEQUENCE   257 AA;  28182 MW;  CA9BDEB6F7ED0029 CRC64;
     MTRFRPCIDL HSGQVKQIVG GTLSTVEADL KTNFVSEHAA AHYANLYRKA NLEGAHVILL
     GPRNEKAARE ALAAWPGKLQ VGGGINEKNA KEWIEAGAER VIITSYLFPE GKFSMERLEA
     VLTALGGDKA KLVIDLSCRR SGSTWFVAMN KWQTITEMEI TQETIKLLEP FCSEFLIHAA
     DNEGLQQGID VDLVQRLSEW CSIPVTYAGG ARTVEDLDLV KDLSKGRVDL TIGSALDVFG
     GSGAKFEDCV AWNRKNS
//
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