ID G8BHA5_CANPC Unreviewed; 612 AA.
AC G8BHA5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN OrderedLocusNames=CPAR2_500550 {ECO:0000313|CGD:CAL0000147089,
GN ECO:0000313|EMBL:CCE43829.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE43829.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC Evidence={ECO:0000256|ARBA:ARBA00001792};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the TPA1 family.
CC {ECO:0000256|ARBA:ARBA00007443}.
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DR EMBL; HE605207; CCE43829.1; -; Genomic_DNA.
DR AlphaFoldDB; G8BHA5; -.
DR STRING; 578454.G8BHA5; -.
DR EnsemblFungi; CPAR2_500550-T; CPAR2_500550-T-p1; CPAR2_500550.
DR CGD; CAL0000147089; CPAR2_500550.
DR VEuPathDB; FungiDB:CPAR2_500550; -.
DR eggNOG; KOG3844; Eukaryota.
DR Proteomes; UP000005221; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0008198; F:ferrous iron binding; IEA:EnsemblFungi.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0019826; F:oxygen sensor activity; IEA:EnsemblFungi.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IEA:EnsemblFungi.
DR GO; GO:0008143; F:poly(A) binding; IEA:EnsemblFungi.
DR GO; GO:0140311; F:protein sequestering activity; IEA:EnsemblFungi.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:EnsemblFungi.
DR GO; GO:2000639; P:negative regulation of SREBP signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:EnsemblFungi.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:EnsemblFungi.
DR GO; GO:0006449; P:regulation of translational termination; IEA:EnsemblFungi.
DR GO; GO:0006415; P:translational termination; IEA:EnsemblFungi.
DR Gene3D; 3.60.130.20; Oxoglutarate/iron-dependent oxygenase, C-terminal degradation domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR043044; TPA1/Ofd1_C.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR PANTHER; PTHR12117; HISTONE ACETYLTRANSFERASE COMPLEX; 1.
DR PANTHER; PTHR12117:SF0; PROLYL 3-HYDROXYLASE OGFOD1; 1.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005221};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 146..252
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 70470 MW; 7C1A3A5E2F4E3544 CRC64;
MAPSKRPQET AVAEEESSPK KLNTNFTKED IEHFFNAQIW KSEFQDEIQK QVKESSPYKW
GTIKHLMDDT LLRQVRKEVL SEIAFTKKET DIYKVYQSGD LANLSGLDWN DLSRLPSLYK
LRAAIYSQEF RDVVSRITGC GKLSGVKTDM SINTYTKGCH LLTHDDVIGS RRVSFILYMP
DPDKVWKPQY GGALRLFPAV VPNVPHTDYE CKLVPQFNQI AFFTVQPGLS FHDVEEVREE
KHRLSIQGWF HIPQPGEDGF VEGEQEKTEA MSTLQQLQSK ELQEFDFPKS IRTEINPLEM
KNIQSCERLN QQDIDYLKYF INPTYLNPTH IRKLSEFFID ESLVELKDFF NDDYASVLKQ
LLRDVEINTE TPQNSTEVRH PWKIAVPPHK QRFMYIDGTS YHGLSKGEIK HINEVGPQEQ
PNFTLLKQSN NLNPTDSKII EICEFLKSVA FKKWLKILTG LILANEQILA RRFRPGHDFI
LATTVDSDAG RNDYEENVLL EATLNLTPTA ATGKKSNSWE SGEFGGYELC MAQNTNDGDE
EDDPAIYRSS KDSEEDSVLY TSQCKWNTLT LMVRDASLLK FVKYVSINAK GSRWDISCQW
NIKAETEEET EN
//
