ID A0A0Q4MGD5_9GAMM Unreviewed; 774 AA.
AC A0A0Q4MGD5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Biotin transporter BioY {ECO:0000313|EMBL:KQN54964.1};
GN ORFNames=ASF13_11060 {ECO:0000313|EMBL:KQN54964.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN54964.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN54964.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN54964.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN54964.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN54964.1,
RC ECO:0000313|Proteomes:UP000050856};
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:KQN54964.1}.
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DR EMBL; LMLK01000023; KQN54964.1; -; Genomic_DNA.
DR RefSeq; WP_056239109.1; NZ_LMLK01000023.1.
DR AlphaFoldDB; A0A0Q4MGD5; -.
DR STRING; 1736225.ASF13_11060; -.
DR Proteomes; UP000050856; 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 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050856}.
FT DOMAIN 11..47
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 52..508
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 624..744
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 709..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 85056 MW; 53A0194E0CFC06E2 CRC64;
MKDEHHLAVM HWGTYRVATD NGTITSVSPV EWDKNPSRIG QSLADGVTSE ARVKRPSVRL
GYLQHGPASR EGRGKEPFVE VSWEVALDLV AREMRSVKAR CGNEAIFGGS YGWASAGRFH
HAQSQLHRFL KGFGGYTAST NTYSSAAGER VLPHILGPLS PLHRQHTHWS ELERECQLFV
AIGGLPLRNA QVNGGAANDH MLKHWLDRLQ QRGVRFINIS PVKNDLSAVP DARWLAIKPG
TDTALLLALC QVLVSEDLVD HGFIASHTVG FAPFRAYLLG ESDGVVKTPQ WAAAITGLDA
GDITALARTM AASRTMINIS WSIQRARQGE QAYWATVALT ALLGQIGTPG GGLAFGYACT
NLAGAARAVF SGPRLPAGKN QVNSVIPVAR LSDMLLNPGG EYAFDGQTLR YPDIRLVYWA
GGNAFHHHQD LNRLVEAWRQ PETVVVNEQY WTAQARHADI ILPVTTSLER EDIGSGGHDG
FMIAMRQLIA PVAEARDDYA IFCGLAERLG FGERFSEGRS PAAWLRKLYD DSRPRAQEEG
ITLPPFDDFW QQGVLEYAPP AKPQVFLAEF RADPQRYPLS TPSGKIELFS DTVAAFGYRE
CPGHAWWDDE EAQYQQQQAQ QWPLHLLSSQ PRTRLHSQFD HGSVSRATKI QGREPLWMHP
DDAAARGITH GSVVRVFNQR GAILAGAQVS DQILRGVVQI STGAWYDPLD PSQPGSLDKH
GNPNVLTEDR GSSRLGQGCS AQSCRVEIEA WREPLPPITV FDQPAFTASP QDVG
//
