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Database: UniProt
Entry: A0A1Y2FSA1_PROLT
LinkDB: A0A1Y2FSA1_PROLT
Original site: A0A1Y2FSA1_PROLT 
ID   A0A1Y2FSA1_PROLT        Unreviewed;       269 AA.
AC   A0A1Y2FSA1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=BCR37DRAFT_126354 {ECO:0000313|EMBL:ORY86829.1};
OS   Protomyces lactucae-debilis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC   Taphrinales; Protomycetaceae; Protomyces.
OX   NCBI_TaxID=2754530 {ECO:0000313|EMBL:ORY86829.1, ECO:0000313|Proteomes:UP000193685};
RN   [1] {ECO:0000313|EMBL:ORY86829.1, ECO:0000313|Proteomes:UP000193685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12-1054 {ECO:0000313|EMBL:ORY86829.1,
RC   ECO:0000313|Proteomes:UP000193685};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORY86829.1}.
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DR   EMBL; MCFI01000002; ORY86829.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2FSA1; -.
DR   STRING; 56484.A0A1Y2FSA1; -.
DR   OMA; IEWNKTH; -.
DR   OrthoDB; 312953at2759; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000193685; 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:ORY86829.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193685}.
SQ   SEQUENCE   269 AA;  29139 MW;  F9A7ABC26917F24E CRC64;
     MSARQTLFRP CIDIHSGVVK QIVGGTLTEQ KDSHASDSLK TNWVSTRPAS YYANLYKEHN
     LEGGHVIMLG PGCEDAATEA LQAWPNRLQV GGGINDTNAV KWLSAGASKI IVTSWLFPDA
     QFSSQRLDAL VSLVGKEALV VDLSCRRKKD GHGWTVAMNK WQTLTTLDIN DANLDMLADR
     CSEFLIHAAD VEGLQGGIDE ELVQYLGHWA KQHKDPISIT YAGGARSVED LERVSDLSGG
     LVDLTIGSAL DIFGGQGASL SDCVAFNRR
//
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