ID E6ZW79_SPORE Unreviewed; 524 AA.
AC E6ZW79;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000256|ARBA:ARBA00018464};
DE EC=5.3.1.16 {ECO:0000256|ARBA:ARBA00012550};
DE AltName: Full=5-proFAR isomerase {ECO:0000256|ARBA:ARBA00031376};
DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000256|ARBA:ARBA00030547};
GN ORFNames=sr11343 {ECO:0000313|EMBL:CBQ71486.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ71486.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ71486.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family.
CC {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|RuleBase:RU003657}.
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DR EMBL; FQ311444; CBQ71486.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZW79; -.
DR EnsemblFungi; CBQ71486; CBQ71486; sr11343.
DR VEuPathDB; FungiDB:sr11343; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG3055; Eukaryota.
DR HOGENOM; CLU_039330_0_0_1; -.
DR OrthoDB; 312953at2759; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000008867; Chromosome 22.
DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03046; GST_N_GTT1_like; 1.
DR CDD; cd04723; HisA_HisF; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR011858; His6-like_euk.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR044524; Isoase_HisA-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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; PF02798; GST_N; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003657};
KW Histidine biosynthesis {ECO:0000256|RuleBase:RU003657};
KW Transferase {ECO:0000313|EMBL:CBQ71486.1}.
FT DOMAIN 11..93
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
SQ SEQUENCE 524 AA; 56987 MW; 186AA4F9190095E6 CRC64;
MSGTTASAAT SPGLVLHHLE LSRSNRILFL LEELQVPYSL KHYKRDPVTR LAGDDLKQVH
PLGRSPVLTD GDLTIIETNA IIEHLLQHYY DPARVALGPR LGEKTQVSID VSAWIQFAEA
SIMLHAIPLF YVIKGGAATE DGSAGVEKVC ARGIKADLAY VEETLARNSG QLVKGCEFSA
ADCAMLYSVD MVGHILGTRS EQWRSNLGLG LGPATNKWMD KCFQRPAFQA ALRKEGIPEG
QDDWLAAFFG GASASSTSQA PKRTRKSLFR PCIDLHEGVV KQIVGGTLTD TDSTLKTNFV
ATHSPAYFAS LYRQHKLTGG HVIKLGPRND QAATAAVSAW PQGLHVGGGI NGDNASEWIQ
RGAEKVIVTS YLFPGCKFSL ERLQELSAKV GKQNLVVDVS CRKKGDRWIV AMNRWQDMTD
MEVNRQSLDL LADHCSEFLI HAADVEGLCQ GIDQELVAKL GEWVTIPTTY AGGARHIGDL
ELVDRLSRGK VDLTFGSALD IFGGSGVTLD ELVRWNESAH TDAA
//
