ID Q5LQU6_RUEPO Unreviewed; 760 AA.
AC Q5LQU6;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Oxidoreductase, molybdopterin-binding protein {ECO:0000313|EMBL:AAV95647.1};
GN OrderedLocusNames=SPO2389 {ECO:0000313|EMBL:AAV95647.1};
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV95647.1, ECO:0000313|Proteomes:UP000001023};
RN [1] {ECO:0000313|EMBL:AAV95647.1, ECO:0000313|Proteomes:UP000001023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2] {ECO:0000313|EMBL:AAV95647.1, ECO:0000313|Proteomes:UP000001023}
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000031; AAV95647.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5LQU6; -.
DR STRING; 246200.SPO2389; -.
DR PaxDb; 246200-SPO2389; -.
DR KEGG; sil:SPO2389; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_5; -.
DR Proteomes; UP000001023; 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 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:UP000001023}.
FT DOMAIN 20..59
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 64..519
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 635..750
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 760 AA; 82956 MW; 956ED80C0A9DF099 CRC64;
MAQSTRKGSI MSKQTRELLT STHWGTYRVE VKDGKVTALR GFEEDPDPSA IGPGIVDVLD
GPTRITAPMV RKGWLEGGPG AAGDRRGADD FVEITWDEAN RIVANELDRV RKTHGNRAIY
AGSYGWASAG RFHHAQSQLK RFLNCIGGFT GSKNTYSFAA AEVVVPHILG DFRTYIDTTT
SWASIASDCE LFVAFGGVPL KNGQISQGGT GAHVQRGGLL AAHEAGVRFV NISPLRSDIL
DRVGADWLAI RPSTDVALML ALAHVLLNEG LHDPDFLDRF TVGFDRFAAY LRGGTDGQAK
TPEWAAEICG IPAGTIAKLA RDMAASRTMI STAWALTRQD HGEQPFWAAI ALAAMLGQIG
LPGTGIGFGY SAMNNTGLNR RQINYASFPQ GRNPVPDFIP VARVTEMLEN PGGRFEYDGK
TYEYPDIRLV WWAGGNPFHH HQDLNRMRRA WARPETIIAN EWCWNALAQH ADIVLPCTTP
LERSDIALTP KDPYQVVMDQ AILPVGQARD DHGIFRGVAA EMGVEDMFTE GKSAGEWQRW
LWDVSRQQAA EQGVELPGWD RLQRDGWIRV PAPAAPTIML EAFRTDPTAN PLATPSGKIE
IYSETIAGFG YDDCPGHPAW MEPAEWLGRA DPGQLHMISN QPRNKLHSQL DHGSVSRADR
PKGVEPVMMH PADAAARKLT GGQIVRLHNT RGACLAELRL SDAIRPGVIQ IATGAWLDPQ
GDLCRRGNPN MLTLDKGTSK LAQGPIAHSC LVMVEACAEA
//
