ID A0A0K9PT33_ZOSMR Unreviewed; 333 AA.
AC A0A0K9PT33;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamilyprotein {ECO:0000313|EMBL:KMZ72203.1};
GN ORFNames=ZOSMA_16G01760 {ECO:0000313|EMBL:KMZ72203.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ72203.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
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:KMZ72203.1}.
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DR EMBL; LFYR01000643; KMZ72203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PT33; -.
DR STRING; 29655.A0A0K9PT33; -.
DR OMA; ARETGFF; -.
DR OrthoDB; 101125at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF34; 2-OXOGLUTARATE-DEPENDENT DIOXYGENASE 33; 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|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987}.
FT DOMAIN 185..289
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 333 AA; 37323 MW; BE9186D7DE691FBA CRC64;
MMVTSNFTTI PIIDVAPLLA KCDDPNGTDD KDLLEVVAML DEACRGVGFF YLKGHGVPDS
LVRDVRDSTR SFFRLQDEEK LKIKLTSKSG FRGYQLIKEN ITKGLPDLHE AIDLYKEIEP
GMYGQLGTTL VGSNQWPENP TRMKSVMEKY VDLLKEVSRK IMRGIALALG GPVDTFEQEQ
MAGDQFWVMR LIGYPGSNSN SKNTDSVGCG AHTDYGLLTL VNQDESSSAL EVKNQNDEWI
SAVPIPGTFV CNIGDMLQVW SNGEYRSTVH RVIVDSPKYR VSVPFFYEPN FDAAVEPLEF
CKSRNGGVAR FEKVVYGEHL VRKVLTNFVS YDF
//
