ID A0A011PVV9_9PROT Unreviewed; 469 AA.
AC A0A011PVV9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative FAD-linked oxidoreductase {ECO:0000313|EMBL:EXI70469.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:EXI70469.1};
GN ORFNames=AW07_04072 {ECO:0000313|EMBL:EXI70469.1};
OS Candidatus Accumulibacter sp. SK-11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454000 {ECO:0000313|EMBL:EXI70469.1, ECO:0000313|Proteomes:UP000020226};
RN [1] {ECO:0000313|EMBL:EXI70469.1, ECO:0000313|Proteomes:UP000020226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-11 {ECO:0000313|Proteomes:UP000020226};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-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:EXI70469.1}.
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DR EMBL; JFAW01000038; EXI70469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011PVV9; -.
DR STRING; 1454000.AW07_04072; -.
DR PATRIC; fig|1454000.3.peg.3339; -.
DR Proteomes; UP000020226; 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:EXI70469.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020226}.
FT DOMAIN 37..218
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 469 AA; 49114 MW; B3B7C23EF33805BA CRC64;
MDKAALIGKL GEVVGEANVL VAADAIAGHL VDWRGRYRGR AVCVVRPANT AAVSAVVRLC
AQAGVAMVPQ GGNTSLCGAA TPAVDGSSVV ISLARLNRVR AIDAANNTIT VEAGCLLQRV
QEAAAAAGRL FPLSLAAEGS CQIGGNLSTN AGGVQVLRYG NARELTLGLE VVLASGEIWD
GLRGLRKDNT GYDLKHLFIA AEGTLGIITA AVLKLFPWPR ARATAWLAIA APATAVGLLT
ALQDRFGPAL TACELVSDVA LALVRKHIPG SHPVLADSPW HLLVELSGGG DELVLREALA
SFLAGAIEDR SIADAVLAQS GEQARRLWTL RESIGEAQRI EGPSIKHDVS LPVSCLPDFV
ERADGALVEA FPGIRMVTFG HVGDGNLHYN QSQPAVGDNA AFLAAQPQVD RLVHDLVHEL
GGSISAEHGI GQLKRAELLR YRSPVEIGMM RAIKEALDPR GLMNPGKLL
//
