ID A0A0C3CQ28_HEBCY Unreviewed; 269 AA.
AC A0A0C3CQ28;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-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=M413DRAFT_441260 {ECO:0000313|EMBL:KIM46189.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM46189.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM46189.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-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}.
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DR EMBL; KN831771; KIM46189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3CQ28; -.
DR STRING; 686832.A0A0C3CQ28; -.
DR HOGENOM; CLU_065050_0_0_1; -.
DR OrthoDB; 312953at2759; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000053424; 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:UP000053424}.
SQ SEQUENCE 269 AA; 29472 MW; 275F20D8796E5BA0 CRC64;
MTPRCSLFRP CIDLHQGQVK QIVGGTLSDK SPDTLKTNFV ARQSAGEFAR IYKENNLEGG
HVIKLGPGND EAALDALSSW PGGLQVGGGI NEKNARYWID AGASKVIVTS FLFPDGRFSL
EHLKSISEIV GKGRLVVDVS CRRRGDRWLV AMNKWQDITD MEVSQNSLDM LSEYCSEFLI
HAADVEGLCQ GIDEDLVRKL GEWVTIPTTY AGGARDISDL DLVHRLSGGR VDLTYGSSLD
IFGGAQVKFQ DLVKENTLRQ AKNQGNEGV
//