ID A9C3C5_DELAS Unreviewed; 1017 AA.
AC A9C3C5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ABX37236.1};
GN OrderedLocusNames=Daci_4607 {ECO:0000313|EMBL:ABX37236.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX37236.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX37236.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000884; ABX37236.1; -; Genomic_DNA.
DR RefSeq; WP_012206406.1; NC_010002.1.
DR AlphaFoldDB; A9C3C5; -.
DR STRING; 398578.Daci_4607; -.
DR GeneID; 24118144; -.
DR KEGG; dac:Daci_4607; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_010756_1_0_4; -.
DR OMA; QDIIWHS; -.
DR Proteomes; UP000000784; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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 PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF119; OXIDASE-RELATED; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784}.
FT DOMAIN 50..282
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 658..690
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1017 AA; 111853 MW; 6297A70FE4D0C23E CRC64;
MSIAPLPHAS APVPAQYLEF LEALKATGFE GDVDTDHASR TVLATDNSIY QRMPQAAIYP
RHSEDVARAA QVLARPEFRD VVLTPRGGGT GTNGQSLTHG VTMDLSRHMN GILEINAEQR
WVRVQAGVVK DQLNAALKPY GLFFAPELST SNRATIGGMI NTDASGQGSC TYGKTRDHVL
ALDFVLLGGE RLHSAPLDAE ALERMCADSG RIGKVHRTAR RISEDQAELI EARFPKLNRC
LTGYDLAHLR EGDGRFNLNS VLCGAEGSLG FVVEARLNVL PIPRYSVLVN VRYAGFMDAL
RDARALMAHR PLSIETVDSK VLLLAMKDFV WSSVAEYFPQ DGQRPTLGIN LVEFSGDDPQ
EVDGRVQAFL GHLGADASVE RLGHTLAAGN AAVHRVYAMR KRAVGLLGNV AGEARPQPFV
EDTAVPPENL PEFIAEFRAL LDSHGLQYGM FGHVDAGVLH VRPILDMKNP VDAALVRPIS
DAVAELTQRH GGLLWGEHGK GLRSEYVPAF FGELYPSLQQ LKAAFDPHNQ LNPGKIATPP
ASKTLLLKVD GVTTRGELDR QIDERVWQSY GAAMHCNGNG ACYNFDPDDA MCPSWKATRQ
RVHSPKGRAS LMREWLRLQG QAGVNVLEVA QRPQPFLSSL AARWRNSRAA RRGEADFSHE
VYDAMAGCLA CKSCAGQCPV KVNVPEFRSR FLELYHRRYL RPVRDYLIGS LEFTMPWLAR
MPALYNGVMG SPWMRDVLSR RIGMVDGPLL SRLDLAATLR QWKVRAADAQ ALAALTPEQR
ARSVVIVQDS FTRYFETGQL QVLIELAARL GFQVWLAPLL PNGKPLHVQG FMGAFARAAI
RNAAQLAQLA QSGVALVGLD PAMTLAYRQE YLKVPGMGEV PKVALPQEWL LQVLPEAVTS
VASVAYRLLP HCTEKTNAPD SGKQWTQLFE RRGLRLSVEA TGCCGMSGTY GHEARNLETS
KTIYAQSWEK QIESKQNLGE PLATGYSCRS QVKRLSARQV RHPLEALLDH VRATHQG
//