ID A0A0S3SUY9_PHAAN Unreviewed; 356 AA.
AC A0A0S3SUY9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN Name=Vigan.08G358100 {ECO:0000313|EMBL:BAT96614.1};
GN ORFNames=VIGAN_08358100 {ECO:0000313|EMBL:BAT96614.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT96614.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT96614.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP015041; BAT96614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3SUY9; -.
DR Proteomes; UP000291084; Chromosome 8.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; 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; PTHR10209:SF450; AMINOCYCLOPROPANECARBOXYLATE OXIDASE; 1.
DR PANTHER; PTHR10209; OXIDOREDUCTASE, 2OG-FE II OXYGENASE FAMILY PROTEIN; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084}.
FT DOMAIN 206..306
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 356 AA; 40326 MW; 17F0EE3BB050FF91 CRC64;
MEDSKRVEEL KAFDDTKLGV KGLVDEGITK IPSIFHHPLD NIKRVSESGH KDYTIPIIDL
GRIHEDSGER KRVVERVKEA SETWGFFQIV NHGIPVSTLE EMLDGVVRFF EQDSEVKKEF
YTRDKKPFIF NSNFNLYSNA PANWKDTFIC DRTTNLPTLG DLPSVCRDIL VEYTDEVSKL
GSLLFELLSE GLGLDRTYLA DIGCNGGLYA VGHYYPPCPE PELTMGITKH ADVDFITVLL
QNQIGGLQVL HQDMWIDLPP LPEALVVNIG DFLQLLSNDK FKSAQHRVLA NRVSPRVSIA
CFLTTSSHSN ARIYGPIKEL LSEENPAKYR EFSVPEFLAH YSKCANQIPP LMHFRI
//