ID H0FEA4_9BURK Unreviewed; 473 AA.
AC H0FEA4;
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 4 {ECO:0000313|EMBL:EHK63340.1};
GN ORFNames=KYC_25578 {ECO:0000313|EMBL:EHK63340.1};
OS Achromobacter arsenitoxydans SY8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK63340.1, ECO:0000313|Proteomes:UP000003113};
RN [1] {ECO:0000313|EMBL:EHK63340.1, ECO:0000313|Proteomes:UP000003113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8 {ECO:0000313|EMBL:EHK63340.1,
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:EHK63340.1}.
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DR EMBL; AGUF01000082; EHK63340.1; -; Genomic_DNA.
DR RefSeq; WP_008167805.1; NZ_AGUF01000082.1.
DR AlphaFoldDB; H0FEA4; -.
DR STRING; 477184.KYC_25578; -.
DR PATRIC; fig|477184.5.peg.5028; -.
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 InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
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;
FT DOMAIN 36..217
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 473 AA; 49774 MW; ACA459BB48C936A6 CRC64;
MTRAALLADL IACLGESNVL TGEDAAPYLT DWRRTVTGRA LAVLRPGDSG EVARVVRLCA
AAGVPVVPQG GNTGQVAAAT PDASASAVVL SLARMNRVRA VDLDNDTITV EAGCVLQAVQ
EAARQAGRLF PLSLGAQGSC TIGGNLATNA GGTQVLRYGN ARELALGLEV VTPQGEIWDG
LRGLRKDNTG YDLRDLYIGS EGTLGVITAA VLKLFPLPRA QRTALIAVPG LPQALQLLQR
ARAGFGAGLT AFEVMSAACM RDVVQAFPLQ RMPFADLPGD AWCALLEVSD SEDEQHAQER
LEAVLAAALE EGEALDAAVS VSGAQSAAFW HLRESITLAL AQARACVKHD ISLPASRIPD
FVQSTDAALA AAFPGVAMRV FGHLGDGNLH YNLLPPEGAS QTDIQRLVHD RVHQAGGSIS
AEQGIGQRRV QDLQRYKSVV ELDLMRRIKR ALDPQGLMNP GKVLSADSDG VLP
//
