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
//