ID   D6ZKK5_MOBCV            Unreviewed;       981 AA.
AC   D6ZKK5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=FAD linked oxidase, C-terminal domain protein {ECO:0000313|EMBL:ADI67254.1};
GN   OrderedLocusNames=HMPREF0573_10935 {ECO:0000313|EMBL:ADI67254.1};
OS   Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio
OS   vaginalis).
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Mobiluncus.
OX   NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI67254.1, ECO:0000313|Proteomes:UP000006742};
RN   [1] {ECO:0000313|Proteomes:UP000006742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43063 / DSM 2711 / V125
RC   {ECO:0000313|Proteomes:UP000006742};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT   "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL   Submitted (MAR-2010) 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; CP001992; ADI67254.1; -; Genomic_DNA.
DR   RefSeq; WP_013189035.1; NC_014246.1.
DR   AlphaFoldDB; D6ZKK5; -.
DR   STRING; 548479.HMPREF0573_10935; -.
DR   GeneID; 55565072; -.
DR   KEGG; mcu:HMPREF0573_10935; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_010756_0_0_11; -.
DR   Proteomes; UP000006742; 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   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 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:UP000006742}.
FT   DOMAIN          21..237
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          583..611
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   981 AA;  105706 MW;  4EDF1C7017768E9F CRC64;
     MVKYLQDPLN RAIYSTDASN YRIVPDRIAQ PKDLDQLRDT ILEALSTGVP LTMRGRGTSC
     SGNSIGPGLV IDTSHHCNRI LSFDPSARQI TVEPGVVLAD IQKVGAPFGL RFGPDPSTWT
     RATVGGSIGN NACGPHAQAW GRVADNVISL DVIDGFGREF TAASGAGALD AVPGLQRLVD
     ENLALIRTEC GRFHRQVSGY SLEHLLPENG RDLAKFLVGS EGTLVSVLRA TLRLVPVPTA
     PVMVVLGYPD MIAAATDVPL INDFSPLAVE GMDSRLVYTL AQKPGVGELP ELPEGNAWLL
     VEMGSATEDL ETTLARANDL AQAANTRATL VLPPSTQATK LWRIRADGAG LGGRTPLNPD
     GSGNDPAWPG WEDAAVPPQN LAAYLRDFTD LMREMNVDGM LYGHLGDGCL HVRLNLPLGA
     EAGQGRSREF LERAADLVGK HHGSLSGEHG DGRARSELLP RMYSPALIDL FKQVKALFDP
     RGLLNPGVLV DPDSLDQNLR LAAAQVIPAL PGQGFTFPKD KDFTAAVHRC TGVGKCLAMN
     QVKNAWMCPS YLATGQEKDA TRGRARVLQE VTNGTLIKNF RDPNLLRALD LCLACKACST
     ACPTGIDMAA YKSESLYRAY RRSLRPRSHY LLGRLPGWLR LARRIPGGAG LANSVFGVGW
     IRRLVFRLFG LDPSRQMAHF ASESFRTWTR RHGGYAAEPE FDTDGLVSPH TDSTPEATER
     VNVAAASARE GSQPAPEAKP WVAVWADSFS EGIAPDGAEA VVELLETAGY QVYVPRPACC
     GLTYVTTGQL DKARHNMRHL CQILGPLAVN GIPIVGVEPS CTATLRDDLE RLLPDDPRAH
     AIARATRTLA ELLSDPETAP NPDVWQLPDL RGVQVVAQPH CHHYSVLDWE TDRKLLAATG
     AEVVELAGCC GMAGNFGMER GHVEVSKRIA EHALLPALRE HTNAIFLADG FSCRTQAEQL
     AGSHGIHLAR LLLGPSARVE A
//