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Database: UniProt
Entry: A0A0B3SCV2_9RHOB
LinkDB: A0A0B3SCV2_9RHOB
Original site: A0A0B3SCV2_9RHOB 
ID   A0A0B3SCV2_9RHOB        Unreviewed;       471 AA.
AC   A0A0B3SCV2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=FAD linked oxidase-like protein {ECO:0000313|EMBL:KHQ54526.1};
GN   ORFNames=OA50_01121 {ECO:0000313|EMBL:KHQ54526.1};
OS   Mameliella alba.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Mameliella.
OX   NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ54526.1, ECO:0000313|Proteomes:UP000030960};
RN   [1] {ECO:0000313|EMBL:KHQ54526.1, ECO:0000313|Proteomes:UP000030960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ54526.1,
RC   ECO:0000313|Proteomes:UP000030960};
RA   Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.;
RT   "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from clonal
RT   culture of toxic dinoflagellate Alexandrium tamiyavanichii.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:KHQ54526.1}.
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DR   EMBL; JSUQ01000003; KHQ54526.1; -; Genomic_DNA.
DR   RefSeq; WP_043138325.1; NZ_JSUQ01000003.1.
DR   AlphaFoldDB; A0A0B3SCV2; -.
DR   STRING; 561184.SAMN05216376_105291; -.
DR   PATRIC; fig|1515334.3.peg.1123; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000030960; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 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; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030960}.
FT   DOMAIN          37..219
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   471 AA;  49814 MW;  E3B345B2A5A3473C CRC64;
     MPLAPADHAF VQRLSALLPD DTLRPAEARH REEPRGRWTS TAEWIALPRS TEEVSTIVRT
     CAETGVGIIP LGGGTGLVGG QLKPDGPAPL IVSLERMSAI RSVHPQENAA VVQAGAILAD
     VQSAAADVDR LFPLSLASEG SARIGGLLGT NAGGINTLRY GNARDQVLGL EAVLPDGSVW
     HGLKRLRKDN TGYDLRHLLI GTEGTLGIIT AASLKLAPRP AATGTALLTV PSPDAALTLL
     ALARGQLGET ISAFELMHRT GFDFLAEKLP DLRQPWDTPP EWSVLMDIGL GRGADPAEAL
     ETLFAAAHEA DLVTDGIVAQ SLAQSEALWT LREHMSEANR LVGAVSSHDI SVPLGAIPEF
     ISRAGPALAR LGDWRINCFG HAGDGNLHYN VFPVPGRTKA DHVDQRDAIK TCVHDLVHEL
     GGSVSAEHGI GRLKVDDLER YGDPAKLAAM RTIKSALDPK GIMNPGAVLR G
//
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