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Database: UniProt
Entry: M5E8F2_9GAMM
LinkDB: M5E8F2_9GAMM
Original site: M5E8F2_9GAMM 
ID   M5E8F2_9GAMM            Unreviewed;       467 AA.
AC   M5E8F2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:CCU73640.1};
GN   ORFNames=TOL_3244 {ECO:0000313|EMBL:CCU73640.1};
OS   Thalassolituus oleivorans MIL-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Thalassolituus.
OX   NCBI_TaxID=1298593 {ECO:0000313|EMBL:CCU73640.1, ECO:0000313|Proteomes:UP000011866};
RN   [1] {ECO:0000313|EMBL:CCU73640.1, ECO:0000313|Proteomes:UP000011866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIL-1 {ECO:0000313|EMBL:CCU73640.1,
RC   ECO:0000313|Proteomes:UP000011866};
RX   PubMed=23599290; DOI=10.1128/genomeA.00141-13;
RA   Golyshin P.N., Werner J., Chernikova T.N., Tran H., Ferrer M.,
RA   Yakimov M.M., Teeling H., Golyshina O.V.;
RT   "Genome Sequence of Thalassolituus oleivorans MIL-1 (DSM 14913T).";
RL   Genome Announc. 1:1-3(2013).
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}.
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DR   EMBL; HF680312; CCU73640.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5E8F2; -.
DR   STRING; 187493.CN03_16215; -.
DR   KEGG; tol:TOL_3244; -.
DR   PATRIC; fig|1298593.3.peg.3138; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_4_1_6; -.
DR   Proteomes; UP000011866; Chromosome.
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   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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011866}.
FT   DOMAIN          40..219
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   467 AA;  51814 MW;  5B0F4D91EAC0DDB7 CRC64;
     MTTLTQEALI EQLSAIVGTD KVRTDADSLE TFGKDWTKIY PPKPSAIVFP KTTEQVQKIV
     LLANEQSLSL VPSGGRTGLS AGAVAANGEV VISFDYMNQI SEFNAIDRTV KCGAGVVTEQ
     LQVFAEEQGL FYPVDFASAG SSQLGGNIST NAGGIKVIRY GMTRDWVAGL TVVTGKGDVL
     NLNKDLVKNN TGYDMRQLFI GGEGTLGFIT EATMRLTRAP KNLTVLVLGV PEFDAIMSVL
     NTFQGRMDLT AFEFFSDKAM RKVVARGDVP APFETPAEYY ALLEFEAENE DHINTAMEIF
     EYCVEQGWVL DGVMSQSETQ AANLWRLRED ISETISEWTP YKNDISVVVS KVPPFLHEIE
     EVVTREYPDF EIIWFGHIGD GNLHLNILKP DDLAKEVFFQ RCAKVSTWVF EIVEKYAGSV
     SAEHGVGLTK KPYLEYTRSK EELDYMRAVK LVFDPKNVMN PGKLIDL
//
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