ID   S4YMR3_SERPL            Unreviewed;       752 AA.
AC   S4YMR3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Biotin transporter BioY {ECO:0000313|EMBL:AGP45806.1};
GN   ORFNames=M621_20395 {ECO:0000313|EMBL:AGP45806.1};
OS   Serratia plymuthica S13.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=1348660 {ECO:0000313|EMBL:AGP45806.1, ECO:0000313|Proteomes:UP000014900};
RN   [1] {ECO:0000313|EMBL:AGP45806.1, ECO:0000313|Proteomes:UP000014900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S13 {ECO:0000313|EMBL:AGP45806.1};
RX   PubMed=23929484;
RA   Muller H., Furnkranz M., Grube M., Berg G.;
RT   "Genome Sequence of Serratia plymuthica Strain S13, an Endophyte with
RT   Germination- and Plant-Growth-Promoting Activity from the Flower of Styrian
RT   Oil Pumpkin.";
RL   Genome Announc. 1:e00594-13(2013).
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}.
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DR   EMBL; CP006566; AGP45806.1; -; Genomic_DNA.
DR   RefSeq; WP_006327609.1; NC_021659.1.
DR   AlphaFoldDB; S4YMR3; -.
DR   KEGG; sry:M621_20395; -.
DR   PATRIC; fig|1348660.3.peg.4000; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_6; -.
DR   Proteomes; UP000014900; Chromosome.
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; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          9..48
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          52..509
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          625..745
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   752 AA;  83098 MW;  B2B9263AA63E35BD CRC64;
     MSIKRYPQLA HWGAYTAVVE DGRLIRCEPF ADDQDPSPLL DSIAPMVYSD KRIRKPAVRR
     SWLQKREGSD RTLRGREDFV EVDWDLALDL VAEENRRVRD RYGPSGLFTG SYGWSSAGRL
     HHARSLVRRF YFSGGGGVDQ LGNYSWGAAQ FFLPYVIGTF TPLTGRVTSW PSVVEHCELF
     VAFGGLALKN AQVSSGGAAE HTLKPWLQKL AQKGTPVINI SPMRDDCPAF VNAEWIPIRP
     NTDVALMLAL AYEIQRRGAQ DEAFLYSHCV GYEQLADYLR GTDDGVAKTP EWASAITGIP
     AARISLLAQQ LIGVRSFITC SYSVQRAHRG EQPYWMMIAL SAMLGQVGLP GGGFSFGHGS
     MNGVGNPRVD TPGPMMPVGT NPCGLAIPVA RICDMLLQPG EPYSFRGETL HYPDIHLVHW
     AGGNPFHHHQ QLNRLVEGWQ KPDTVIVQDI WWTPAAKMAD IVLPVTTSLE RNDIGGSSRD
     RYVLAMHQAI APQHQARNDF DIFADLAERL GYREQFTENR DEQAWIESIY QQCGQAQAGT
     GVEWPEFADF WRKGYVELPT PAKEFVFFDD FRADPQANPL QTPSGKIELF SEKIAGYRYA
     DFAPHPQWQP PVEWLGAPQA KEWPLHLISI QPGDRLHSQM DPAPLAQGNK TAGRETLHMH
     PEDAAMRGIA EGAEVQVSNA RGSCLAGVAI TDGVTRGVVL MATGAWFDPG FGAQRLAVEQ
     SGNPNVLTLD IGTSPLTQGP NAMSCLVEVS VR
//