ID H0FD07_9BURK Unreviewed; 470 AA.
AC H0FD07;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=FAD linked oxidase C-terminal domain-containing protein 5 {ECO:0000313|EMBL:EHK63800.1};
GN ORFNames=KYC_23333 {ECO:0000313|EMBL:EHK63800.1};
OS Achromobacter arsenitoxydans SY8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK63800.1, ECO:0000313|Proteomes:UP000003113};
RN [1] {ECO:0000313|EMBL:EHK63800.1, ECO:0000313|Proteomes:UP000003113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8 {ECO:0000313|EMBL:EHK63800.1,
RC ECO:0000313|Proteomes:UP000003113};
RX PubMed=22328747; DOI=10.1128/JB.06667-11;
RA Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.;
RT "Genome sequence of the highly efficient arsenite-oxidizing bacterium
RT Achromobacter arsenitoxydans SY8.";
RL J. Bacteriol. 194:1243-1244(2012).
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:EHK63800.1}.
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DR EMBL; AGUF01000074; EHK63800.1; -; Genomic_DNA.
DR RefSeq; WP_008166953.1; NZ_AGUF01000074.1.
DR AlphaFoldDB; H0FD07; -.
DR STRING; 477184.KYC_23333; -.
DR PATRIC; fig|477184.5.peg.4588; -.
DR eggNOG; COG0277; Bacteria.
DR OrthoDB; 8522822at2; -.
DR Proteomes; UP000003113; Unassembled WGS sequence.
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 37..218
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 470 AA; 50485 MW; 57013C0D0BDEA1FE CRC64;
MSATDFSQRL VQALGPDTVF TDPADIAPWL SDWRGLYNGQ AQAVVRPRTT AEVAACLALC
QEAGVPVVPR GGNTGLCGGA TPDGGARNVV LSLDRMNAVR SIDTVANTMV AEAGAILGNL
RRAAQDAGRL LPLSLAAEDS SQIGGNVATN AGGVNVVRYG MARELVLGLE AVLPTGEIFH
GLRTLRKDNT GYDLKQLLIG SEGTLGVITA VALRLFPRTD VRSVVLAAVE SPAQALQLFE
ILFEQCGARL QAFEYFSGDC LDLVLTHAEG VQEPFDQRYP AYVLVELADT ADEAGLNTLL
ETVIGTALER GLCLDAAVSA SLAQLQTLWK LREEISEAQR ADGPHLKHDV SLPIERIPDF
MESAEARVRA LYPDIRPFIF GHFGDGNLHY NLSRPAGADR NWVAEHGAAI TDAVLDEVNR
YGGSISAEHG IGQLKRDHFL HSKDPVELRL MREIKKVMDP AGIMNPGKLL
//
