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Database: UniProt
Entry: D6YVN3_WADCW
LinkDB: D6YVN3_WADCW
Original site: D6YVN3_WADCW 
ID   D6YVN3_WADCW            Unreviewed;       916 AA.
AC   D6YVN3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=FAD linked oxidase domain-containing protein {ECO:0000313|EMBL:ADI38194.1};
GN   OrderedLocusNames=wcw_0828 {ECO:0000313|EMBL:ADI38194.1};
OS   Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia.
OX   NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI38194.1, ECO:0000313|Proteomes:UP000001505};
RN   [1] {ECO:0000313|EMBL:ADI38194.1, ECO:0000313|Proteomes:UP000001505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505};
RX   PubMed=20531937; DOI=10.1371/journal.pone.0010890;
RA   Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A.,
RA   Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.;
RT   "The Waddlia genome: a window into chlamydial biology.";
RL   PLoS ONE 5:E10890-E10890(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP001928; ADI38194.1; -; Genomic_DNA.
DR   RefSeq; WP_013181910.1; NZ_LVEB01000053.1.
DR   AlphaFoldDB; D6YVN3; -.
DR   STRING; 716544.wcw_0828; -.
DR   KEGG; wch:wcw_0828; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_010756_0_0_0; -.
DR   OrthoDB; 9767256at2; -.
DR   Proteomes; UP000001505; 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   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
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; IPR009051; Helical_ferredxn.
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; PF02754; CCG; 2.
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; 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:UP000001505}.
FT   DOMAIN          32..249
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   916 AA;  101113 MW;  087BCD2218FA55A2 CRC64;
     MTLFNDLKQS IQGTILSDPA SLGIYSVDAS IYEVMPTAVV LPKNINDIRF AVKIAAKHHI
     PITPRGAATG ITGGCLGSGI ILDLSLHLNR ILEINLEQEY ALCEPGVVQD RLNDALRTNG
     YRLGPDTSTG NRATLGGMLA NNAAGARSLK YGRMIDHVLE VEMILATGEI ITFGPNTPVQ
     HPIVQKILQM CNQNKEEIKK RFPSIPRRVS GYNLDALLGD GIPNLCPLIV GSEGTLGVVT
     KIKVAIAPLP KQTSLSVIHF DDMIEGLSEV PRLLSFNPIS LEMIDRNILE AGQTSPALKD
     KLDWLHGNPA MVLVAEFEGD PDQALEKPIG YAQTILKDPK IQEHVWLVRK AGLGLLLSKR
     SYSRAIAFIE DISVDPQNIA EFMQEFLAYL EKKGKRAGIY GHAGSGCLHI RPYIDLRDPK
     ERQTMKQIQE HVADLVMQYG GTLSGEHGDG LVRSWLTSKL YGENIYSLFK QVKEIFDPNH
     LMNPGKIVRA PPFLQNLRKT PVKSLDTFLD FSKEGGIELS ADLCNGNAQC RKKEGTMCPS
     FQATGREYDS TRARAQTLRG ILHGSLSADG LASKELYHVL DLCLQCKGCK SECPSQVDMA
     KMKTEFLHHF HKKHGLTLRD RIFGHIGTIN QISSHFPRLF NAIGKTRPAK KMIETLGITS
     QRELPELALK RFSKWFSKHP KIGGRKILLF NDTFNEFNCP EVGIAAVKVL EKLGYQIISP
     PWTCCGRTLI SKGMLDSAKV QAEKLIATLL PYAKENIPII GLEPSCLLTI KDDFQGLLGY
     ENPDLKIVNA MSQTFDQFIA SHHKLPFQNT KDSVKLHGHC HQKALTGTSS AMKILHTLGN
     PSEIPSGCCG MAGSFGYEKE HYQISMAIGE LKLFPAVRQT EDPIIADGFS CRCQIAHATG
     KTPLHLAQYL ANLKYV
//
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