ID Q6BXT1_DEBHA Unreviewed; 365 AA.
AC Q6BXT1;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 28-JUN-2023, entry version 93.
DE SubName: Full=DEHA2B00484p {ECO:0000313|EMBL:CAG84970.2};
GN OrderedLocusNames=DEHA2B00484g {ECO:0000313|EMBL:CAG84970.2};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG84970.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG84970.2, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
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DR EMBL; CR382134; CAG84970.2; -; Genomic_DNA.
DR RefSeq; XP_456988.2; XM_456988.1.
DR AlphaFoldDB; Q6BXT1; -.
DR STRING; 284592.Q6BXT1; -.
DR GeneID; 2913077; -.
DR KEGG; dha:DEHA2B00484g; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_10_0_1; -.
DR InParanoid; Q6BXT1; -.
DR OMA; GEWKYVP; -.
DR OrthoDB; 1057251at2759; -.
DR Proteomes; UP000000599; Chromosome B.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR47990:SF39; 2OG-FE(II) OXYGENASE FAMILY, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G00800)-RELATED; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PRINTS; PR00682; IPNSYNTHASE.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT DOMAIN 191..300
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 365 AA; 42692 MW; 9F3E7AE980D93F9B CRC64;
MVTKRNLKNI PKEWIPQDET KYDLDWADLT NIDISTFDKP GGKEKLASQL KIALHKDGFW
TVSGTGISEE EMNRSFALGE FFFNNYSEEE KKLQEVNFEE GNYFGYKIKG NKSVFGTDVP
DNVETFNIAK FTKQGFFEEF FKQDFIKEYR EELEGISRKS FEVARKLFVL FALILELDEN
YFVDRHLYDD QSDDHLRFMK YHPREKEEDD RVENTWARGH TDFGSLTLLY NQVVSGLQIR
LSNGEWKYVP SVPGAIICNI GDTLNFWSGG YFKSTIHRVV RPPPDQVDAP RIGVFYFVRP
GDNTKIEIAE SPVLKNLGLY RKIKPIVGTD YVRSRVKDYH DKKDYLKQNN VKFRLGEFEI
EDGFE
//
