ID A0A109JPR4_9BRAD Unreviewed; 774 AA.
AC A0A109JPR4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Biotin transporter BioY {ECO:0000313|EMBL:KWV52973.1};
GN ORFNames=AS156_09395 {ECO:0000313|EMBL:KWV52973.1};
OS Bradyrhizobium macuxiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV52973.1, ECO:0000313|Proteomes:UP000057737};
RN [1] {ECO:0000313|EMBL:KWV52973.1, ECO:0000313|Proteomes:UP000057737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10303 {ECO:0000313|EMBL:KWV52973.1,
RC ECO:0000313|Proteomes:UP000057737};
RA Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
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:KWV52973.1}.
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DR EMBL; LNCU01000081; KWV52973.1; -; Genomic_DNA.
DR RefSeq; WP_066509470.1; NZ_LNCU01000081.1.
DR AlphaFoldDB; A0A109JPR4; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000057737; 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 CDD; cd02769; MopB_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; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 21..61
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 65..522
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 634..749
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 774 AA; 84484 MW; 4A0ED2C59FC4E12D CRC64;
MNETIGYPDP GLDLSEGFKP HTSHWGVFSA RLRENNRLEV RPYGGDPDPN GIIDNFPAAL
RHGARIAQPA IRRGWLERGP GPDDRRGRDE FVSVSWEKAL DLLGGELTRI RDTRGPGAVF
GGSYGWSSAG RFHHAQSQVH RFLNMAMGGY VRSVNSYSSG ASSVLLPQIL AGYEEITKHN
VTWEQIATES EIVLAFGGMA LKNSMVAGGS ISKHVERGAM EAARRRGCEF ILVSPLRDDM
PAEAGAEWLT ATPGTDTALM MGIVHTLVGE GLHDQAFLDR YTEGWPVFLR YLNGEADGQP
KDAEWAASIC GIDASTIRTL ARRLAGRRAL ITVSHSMQRA EHGEQPVWMG MVLAAALGQI
GLPGGGYAYS LGAIGYYGRR VNAVPGPTLG QGRNGVADFI PVARIADMLL NPGATYRYNG
ATRTYPDIRL VYWAGGNPFH HHQDLNRLRK AFARLDTLVV HELAWTATAR HADIVLPSTM
TLEREDIGYS SNDPLMVAMH QIAEPYGLAR DDYDIFADLA ERLGARDAFT EGRTSQQWLR
HLYEPTRASL ATQGLAAPSF EEFWESGSLV VPQHPDDGGK LRRFREDPVA RPLPTPSGRI
EIFSAKIAGH GDADCPGHPV WLEKTDTPKA ASPLFLVANQ PTTRLHSQLD FGGHSTEAKH
RGREVARMNP RDAEPRGIAD GDIIRLFNSR GACLAAVRVT EAIAAGIIQL PTGAWYDPMD
PEDEAPLCVH GNPNVLTRDI GTSSFAQGCT GQLTTVEVER FNGNLPPIRA FDPV
//