ID A0A177H7Y0_9RHOB Unreviewed; 477 AA.
AC A0A177H7Y0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative FAD-linked oxidoreductase {ECO:0000313|EMBL:OAH06377.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:OAH06377.1};
GN ORFNames=pfor_33c3139 {ECO:0000313|EMBL:OAH06377.1};
OS Rhodobacteraceae bacterium SB2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1689867 {ECO:0000313|EMBL:OAH06377.1, ECO:0000313|Proteomes:UP000077333};
RN [1] {ECO:0000313|EMBL:OAH06377.1, ECO:0000313|Proteomes:UP000077333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB2 {ECO:0000313|EMBL:OAH06377.1,
RC ECO:0000313|Proteomes:UP000077333};
RA Poehlein A., Billerbeck S., Voget S., Wemheuer B., Giebel H.-A.,
RA Brinkhoff T., Daniel R., Simon M.;
RT "A new prominent pelagic Roseobacter clade subcluster - CHAB-I-5:
RT biogeography and genomic comparison to other roseobacters.";
RL Submitted (MAY-2016) 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:OAH06377.1}.
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; LGRT01000034; OAH06377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177H7Y0; -.
DR STRING; 1689867.pfor_33c3139; -.
DR PATRIC; fig|1689867.3.peg.3130; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000077333; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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};
KW Oxidoreductase {ECO:0000313|EMBL:OAH06377.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077333}.
FT DOMAIN 42..223
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 477 AA; 50562 MW; E5CE6A945143150A CRC64;
MPNLSTAPSD DVLDQIKAIL GHGGWKAGAE AISYFDDPRG RFCGAAFLVV LPESTQQVSE
IVSLCNREKI ALIPYGGGTG VVAGQLSIET ENMLILSLER MNSISEVSED DCTVTVQAGC
ILAHLHAAAN EKALQFPLSM ASKGSCSVGG NLATNAGGIQ VVRYGNTRDL CLGIEAVLPC
GSILSDLSPL HKDNTGYDLK HLLIGSEGTL GVITAATFKL TPLDPETVTM LCAVSSPTAA
LALYKKLRLN LRESISALEL LSDFGLDLVA SCFSDLKKPF KQDYSWYVLI EAGGAEGIIE
QALGAVADCL DTGLVQDAVI AQSDTQRATL WRLRENTPEA NRLSGAFVSS DTSVPISKVE
AFIHATCAAV KAINPDLRVN TYGHIGDGNI HHNILPPQGV TKAAFLKAEP DAAERIRMVI
NDATVEFGGS ISAEHGIGRL KTQDLEAYVS PVKRRALKAI KSALDPNNIM NPGAVLR
//
