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Database: UniProt
Entry: V2I063_9BURK
LinkDB: V2I063_9BURK
Original site: V2I063_9BURK 
ID   V2I063_9BURK            Unreviewed;       422 AA.
AC   V2I063;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:ESJ11347.1};
DE   Flags: Fragment;
GN   ORFNames=B551_0215215 {ECO:0000313|EMBL:ESJ11347.1};
OS   Cupriavidus sp. HPC(L).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESJ11347.1, ECO:0000313|Proteomes:UP000053474};
RN   [1] {ECO:0000313|EMBL:ESJ11347.1, ECO:0000313|Proteomes:UP000053474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA   Purohit H.J., Agarwal L.;
RT   "Cupriavidus a Desert isolate.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:ESJ11347.1}.
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DR   EMBL; AMPR02000246; ESJ11347.1; -; Genomic_DNA.
DR   AlphaFoldDB; V2I063; -.
DR   OrthoDB; 8712194at2; -.
DR   Proteomes; UP000053474; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053474}.
FT   DOMAIN          1..165
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ESJ11347.1"
SQ   SEQUENCE   422 AA;  45250 MW;  3950B809E96A24B9 CRC64;
     QAVVAAAQRF GVRLVPQGAN TGLVGASTPD AGGEQVVLST ARLKGAITVD PLNQSVTVGA
     GVLLSELNAR LAQDGLFFPV DLGADPTIGG MIAANTGGAR LLKYGDVRQN LLGVEAVLAE
     PAGELLDLNR ALRKNNVGFD FKQLFVGTGG AFGVVTAATL RVYPLPVQTA TALLVPTGVA
     ELEALLLALN AELGDFLSSC EGISREAAQA VVRHLDDVED PFAELEGADY AMLVELSSTM
     PNRAGGVDLE ALLMDFLERH YGTLIGNAVV GKPEALWRLR HSITESIRHE GKIIALDLSV
     PRSRFPAFRA EARALIAARW PWLRIYDFGH LGDGGVHLNM VWPLQDAPAY DDAVAGEVRA
     ELYRLTVERF EGSFSAEHGI GPYNERFYRD FTAHAVLNHV GAMQARLDPR RTLSRLWLGT
     GE
//
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