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Database: UniProt
Entry: X0D2N1_FUSOX
LinkDB: X0D2N1_FUSOX
Original site: X0D2N1_FUSOX 
ID   X0D2N1_FUSOX            Unreviewed;       259 AA.
AC   X0D2N1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, 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=FOQG_00913 {ECO:0000313|EMBL:EXL01031.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXL01031.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXL01031.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXL01031.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) 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}.
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DR   EMBL; JH658362; EXL01031.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0D2N1; -.
DR   eggNOG; KOG3055; Eukaryota.
DR   HOGENOM; CLU_065050_0_0_1; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000030663; 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:EXL01031.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663}.
SQ   SEQUENCE   259 AA;  28360 MW;  10CB707BE7BACE06 CRC64;
     MTKFRPCIDL HAGQVKQIVG GTLDSTSSAL QTNYVSQHPP AHFAQLYRDN DLTGAHVIML
     GPGNEGPAKE ALEAWPGGLQ VGGGINDKNA KEWLNAGAEK VIITSYLFPE GRFSQVRLDA
     VLQALGGDKN KLVIDLSCRR RGEDSWFVAM NKWQTITDME VNQESIKSLE PYCAEFLIHA
     ADNEGLQRGV DEKLVQRLSE WCSIPVTYAG GGRHLEDLEN VKRLSNGKVD LTIGSALDCF
     GGSGVKFDDC VAWNKKQSI
//
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