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Database: UniProt
Entry: A9C3C5_DELAS
LinkDB: A9C3C5_DELAS
Original site: A9C3C5_DELAS 
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
//
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