ID A0A0D6AXI6_RHOSU Unreviewed; 471 AA.
AC A0A0D6AXI6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative oxidoreductase protein {ECO:0000313|EMBL:BAQ67456.1};
GN ORFNames=NHU_00285 {ECO:0000313|EMBL:BAQ67456.1};
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ67456.1, ECO:0000313|Proteomes:UP000064912};
RN [1] {ECO:0000313|EMBL:BAQ67456.1, ECO:0000313|Proteomes:UP000064912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ67456.1,
RC ECO:0000313|Proteomes:UP000064912};
RA Nagao N.;
RT "Genome sequene of Rhodovulum sulfidophilum DSM 2351.";
RL Submitted (FEB-2015) 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}.
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DR EMBL; AP014800; BAQ67456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6AXI6; -.
DR KEGG; rsu:NHU_00285; -.
DR PATRIC; fig|35806.4.peg.290; -.
DR eggNOG; COG0277; Bacteria.
DR Proteomes; UP000064912; Chromosome.
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 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}.
FT DOMAIN 33..211
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 471 AA; 50574 MW; 37533F31506D3C45 CRC64;
MDPIPYLTDL LGPAHVLTGE DTRGHAHDWT GKYKGTPRAL LRPADRDQLA AIVTYAARHR
LPVVPVAGNT GLAGGAYCDG ALMVSVERLN RIREINQRAR SATVEAGVIL SQLHDAAEAQ
DLVFPLSFGA RGSAMIGGVL STNAGGSNVV RYGSTRGLCL GLEAVLPNGR VMDVMSPLHK
DNTGLDLKDL MIGAEGTLGI VTAAVLRLFP RPRAYATAMV AVSDLDAALD LLNRLQEATG
GAVEAFEYMP DDYMRQLFRL RPEMRPPFDR AYPISIMVEI GATAPRDATP GPDGRLPVVQ
LLEDTLGEGF ERGEVLDAVI AQNETQREEI WARREISAEI CFSAAHVVDN DIALPLDRVG
TFLERMTARL PQIDPAAESI TVGHLGDGNL HYTVWASSGS ADLKETIREA VEDEVAALDG
SFSAEHGIGL SKLSTMARRK NPVALDAMRR IKAALDPEGI MNPGKLVPPA D
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