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Database: UniProt
Entry: A0A0Q7APB4_9BURK
LinkDB: A0A0Q7APB4_9BURK
Original site: A0A0Q7APB4_9BURK 
ID   A0A0Q7APB4_9BURK        Unreviewed;       754 AA.
AC   A0A0Q7APB4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Biotin transporter BioY {ECO:0000313|EMBL:KQW37738.1};
GN   ORFNames=ASC76_06470 {ECO:0000313|EMBL:KQW37738.1};
OS   Rhizobacter sp. Root404.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW37738.1, ECO:0000313|Proteomes:UP000051611};
RN   [1] {ECO:0000313|EMBL:KQW37738.1, ECO:0000313|Proteomes:UP000051611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root404 {ECO:0000313|EMBL:KQW37738.1,
RC   ECO:0000313|Proteomes:UP000051611};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW37738.1, ECO:0000313|Proteomes:UP000051611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root404 {ECO:0000313|EMBL:KQW37738.1,
RC   ECO:0000313|Proteomes:UP000051611};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQW37738.1}.
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DR   EMBL; LMDS01000004; KQW37738.1; -; Genomic_DNA.
DR   RefSeq; WP_056464123.1; NZ_LMDS01000004.1.
DR   AlphaFoldDB; A0A0Q7APB4; -.
DR   STRING; 1736528.ASC76_06470; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000051611; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR   InterPro; IPR041460; Molybdopterin_N.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF18364; Molybdopterin_N; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051611}.
FT   DOMAIN          8..43
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          52..506
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          621..740
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          628..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   754 AA;  82140 MW;  3874330ED5312AAB CRC64;
     MSIQRFSHCS HWGAYTLLVE DGRVIGAEPF AGDPAPSPII HSVRHWADPT YRIAQPMVRE
     SWLRHRGPGP RAPGDKFVPV GWDEAAKLVA GEIDRVRTKH GNGSIFAGSY GWTSCGRFHH
     ASSQLKRMMN LVGGYTGHVD TYSIAAGPVI LRHTLGDAEA CGGGANTLDS VAEHAETVIV
     FGALSPRTAQ SEAGGIARHT LEQNLRTMVA RGVRVVLVSP VRDDIPDWVP AEWWPVRPNT
     DTALMLGLAG EIVAAGHHDR DFLARCCSGG EELIGYLNGA QDGVVKNAAW AAAICEIDAE
     RIRELARRVV ATRTMITVSW SLQRADHGEQ PFWAALGLAS AIGQIGLPGG GVGFGYASLG
     GVGAPMAVSR SPSLPQGRNP TADFIPVARI SDLLLNPGQT FTYEGQTRTY PDTRLVLWAG
     GNPFHHHQDL NRLRRAWARP ETIVVQDPVW TATARRADIV LPATSSIERN DISGNKRSDH
     LIAMQQAIAP LGLARNDYDI FRHIADELGV EPAFSEGRDE MAWIRLMYDL TREDAERRLK
     HPMPAFEAFW AEGAARVPTR SNHVFLDRFR ADPAAHPLAT ESGRIVLYSR ELEGLQLADC
     PPHPAWLEPA EWLGRAAPDQ LHLMSRQPQG KLHSQLDDAP AAQASKRDGR EQVWLNPADA
     RRFGIEDGAV VRLFNARGQC LASACVVDTV RPGVAVLPTG AWYDPADEGE NPLERSGNPN
     VLTLDKGTSH FGQGCSAHTC LVSIETHRLQ ETTA
//
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