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Database: UniProt
Entry: A0A2N3NHN7_9PEZI
LinkDB: A0A2N3NHN7_9PEZI
Original site: A0A2N3NHN7_9PEZI 
ID   A0A2N3NHN7_9PEZI        Unreviewed;       293 AA.
AC   A0A2N3NHN7;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=jhhlp_001272 {ECO:0000313|EMBL:PKS11976.1};
OS   Lomentospora prolificans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX   NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS11976.1, ECO:0000313|Proteomes:UP000233524};
RN   [1] {ECO:0000313|EMBL:PKS11976.1, ECO:0000313|Proteomes:UP000233524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS11976.1,
RC   ECO:0000313|Proteomes:UP000233524};
RX   PubMed=28963165; DOI=10.1534/g3.117.300107;
RA   Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA   Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT   "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT   prolificans (Formerly Scedosporium prolificans).";
RL   G3 (Bethesda) 7:3831-3836(2017).
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:PKS11976.1}.
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DR   EMBL; NLAX01000004; PKS11976.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3NHN7; -.
DR   STRING; 41688.A0A2N3NHN7; -.
DR   VEuPathDB; FungiDB:jhhlp_001272; -.
DR   InParanoid; A0A2N3NHN7; -.
DR   OrthoDB; 312953at2759; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000233524; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233524}.
SQ   SEQUENCE   293 AA;  32205 MW;  05FBC12067F64741 CRC64;
     MEGHPAQVLP ELHQNFLIPS TEPPSSPVHF QPLPPAMTRF RPCIDLHAGQ VKQIVGGTLD
     SESAALKTNF VSHLPPAHFS KLYRDSELAG AHVIMLGPGN TEAAREALEA WPGGLQVGGG
     ITDQNAQEWI DAGAEKVIIT SYLFPEGKFS QERLDAVLRN LGNDRSKLVI DLSCRKTGEQ
     SWHVAMNKWQ KITDMEVNQD SIRQLEPYCS EFLIHAADNE GLQKGIDEEL VKRLAEWCTI
     PVTYAGGARH LEDLDQVKSI SNGKVDLTIG SALDCFGGSG VKFDDCVAWN KRQ
//
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