ID A0A2H0ZLV9_CANAR Unreviewed; 612 AA.
AC A0A2H0ZLV9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=B9J08_003216 {ECO:0000313|EMBL:PIS51621.1}, CA7LBN_000770
GN {ECO:0000313|EMBL:QWW22024.1};
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS51621.1, ECO:0000313|Proteomes:UP000230249};
RN [1] {ECO:0000313|EMBL:PIS51621.1, ECO:0000313|Proteomes:UP000230249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS51621.1,
RC ECO:0000313|Proteomes:UP000230249};
RX PubMed=27988485; DOI=.1093/cid/ciw691;
RA Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT continents confirmed by whole-genome sequencing and epidemiological
RT analyses.";
RL Clin. Infect. Dis. 64:134-140(2017).
RN [2] {ECO:0000313|EMBL:PIS51621.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS51621.1};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida auris genome assembly and annotation.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QWW22024.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA7LBN {ECO:0000313|EMBL:QWW22024.1};
RA Finianos M.;
RT "Candida auris outbreak in lebanese hospital.";
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
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; PEKT02000007; PIS51621.1; -; Genomic_DNA.
DR EMBL; CP076749; QWW22024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H0ZLV9; -.
DR STRING; 498019.A0A2H0ZLV9; -.
DR EnsemblFungi; B9J08_003216-t37_1; B9J08_003216-t37_1-p1; B9J08_003216.
DR VEuPathDB; FungiDB:B9J08_003216; -.
DR VEuPathDB; FungiDB:CJI96_0001753; -.
DR VEuPathDB; FungiDB:CJI97_003291; -.
DR VEuPathDB; FungiDB:CJJ07_001238; -.
DR VEuPathDB; FungiDB:CJJ09_000888; -.
DR VEuPathDB; FungiDB:QG37_02086; -.
DR OMA; GWYHIPQ; -.
DR Proteomes; UP000230249; Unassembled WGS sequence.
DR Proteomes; UP000825438; Chromosome I.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IEA:UniProt.
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:UP000230249};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 143..249
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 612 AA; 69883 MW; D07A2B8A59DAED54 CRC64;
MAVEKRPAEE TETTVVKKLN NSFSHDEIVS FLNNKIFEKE FQENLRLDIS QSQPFRWGTV
TELINDELLR SVRTEILGEI AFTKKETDIY KVFQSGDLAN LSGLDWNDLS RLPSLYKLRA
AIYSEEFRDF ISNVTGCGKL SGVKTDMSIN TYTKGCHLLT HDDVIGSRRV SFILYMPDPK
FTWKSHYGGG LRLFPAVVPN VPETDHQVKL VPQFNQMAFF TVQPGLSFHD VEEVRVDKQR
LSIQGWFHIP QPGEDGYIPG EQEATEAKST LQQLQSKELQ EFDFPKPFRN DLYPEEIKEY
ESLNLSSNFF DDTEVEYLGK FLNPTYLNKA SLARLNESFV EESVVEIKEI LKEEYASLLQ
ETLRKTEIEN KVPQTSKEIH FPWKCAVPPH KQRYMYIDGK GDIDLTEKGI NFHNHIGPQE
LPNFELAKGL TQTKPEKMLL ELMQFMKSIS FRKWLTYVTN LVVTSDQILA RKFRPGQDFI
LATTTEKMLA REHNDEVNVL LEATLGLTPT AINAKNWESG EFGGYELCMA TGVGSDGEAE
DDDPAIYKAG DPNDDSVLYS SQCKWNTLCL MVRDPSVLKF VKYVSINAKG SRWDISAQFN
VKALGDDDED GH
//
