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Database: UniProt
Entry: A0A0S1XVI8_9BORD
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Original site: A0A0S1XVI8_9BORD 
ID   A0A0S1XVI8_9BORD        Unreviewed;       529 AA.
AC   A0A0S1XVI8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:ALM81847.1};
GN   ORFNames=ASB57_01700 {ECO:0000313|EMBL:ALM81847.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM81847.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM81847.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM81847.1,
RC   ECO:0000313|Proteomes:UP000064621};
RA   Hou L.;
RT   "Draft genome of Bordetella sp. N.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CP013111; ALM81847.1; -; Genomic_DNA.
DR   RefSeq; WP_057650004.1; NZ_CP013111.1.
DR   AlphaFoldDB; A0A0S1XVI8; -.
DR   STRING; 1746199.ASB57_01700; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000064621; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT   DOMAIN          203..232
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          55..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  57856 MW;  635F1809A647F6FD CRC64;
     MSTEFDADVI VVGSGVCGSL AAHRLGKAGK HVILLEAGPR VPRWKIVEKF RNTPVKGNPN
     GPYPDTSYAP KSDSKGYLEE TGSTKNNPSY LRLVGGTTWH WAGACYRFLP NDFKMQTLYG
     VSRDWPISYE DLEPYYGQAE VELGVSGPDD ADQSATGRAG TYPPRSTPYP MKAQPLPYMQ
     ERADAVLSAA GYRVINEPTA RNSRPYDDRP TCQGNNSCTP VCPIGALYNG SVHAYKSEAV
     GVKLMTDAVV YQVEADGAGK IVAVRYKSPD GSEHRLTARA FVLAAYSIET PRLLLMSNIA
     NSSDMVGRNL SCQPECHQNF MTSEALWPGR GPVHPQTFFT ARDGEFRRER AGTKHVVVNN
     SPNDKIAGNL LKKGIIGPRL DEMIRDQASR IMELSTQHEY PGEPSNRVTL STTRKDALGL
     PTPVVHFNRD NAYFLAGFED TKRVYKRVAE LFGATEYSPL TWVHPHTQGT TIMGADPKTS
     VVDPFGRAHD HPNLYIVGPN VLTTTGTVNP TLTAAALALR TADAVLHSI
//
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