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}.
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; 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
//