ID V2QEY7_9BACT Unreviewed; 951 AA.
AC V2QEY7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Periplasmic nitrate reductase {ECO:0000313|EMBL:USF23887.1};
DE EC=1.9.6.1 {ECO:0000313|EMBL:USF23887.1};
GN Name=napA_2 {ECO:0000313|EMBL:USF23887.1};
GN ORFNames=N508_000960 {ECO:0000313|EMBL:USF23887.1}, N508_00421
GN {ECO:0000313|EMBL:ESJ99120.1};
OS Mucispirillum schaedleri ASF457.
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Mucispirillaceae; Mucispirillum.
OX NCBI_TaxID=1379858 {ECO:0000313|EMBL:ESJ99120.1};
RN [1] {ECO:0000313|EMBL:ESJ99120.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF457 {ECO:0000313|EMBL:ESJ99120.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF23887.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23887.1};
RA Proctor A.L., Phillips G.J., Wannemuehler M.J.;
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF23887.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF457 {ECO:0000313|EMBL:USF23887.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (JUN-2022) 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}.
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DR EMBL; AYGZ01000009; ESJ99120.1; -; Genomic_DNA.
DR EMBL; CP097562; USF23887.1; -; Genomic_DNA.
DR AlphaFoldDB; V2QEY7; -.
DR STRING; 1379858.N508_00421; -.
DR PATRIC; fig|1379858.3.peg.415; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_309683_0_0_0; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000017429; 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 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; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 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};
KW Oxidoreductase {ECO:0000313|EMBL:USF23887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017429}.
FT DOMAIN 5..580
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 841..936
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 951 AA; 105161 MW; A5531AF6D7F1AC32 CRC64;
MGGYAKYTHD YSFHQRSFFG TGYTGYNGSS ANANTVASAV KNVVLWGSNV LSTVNSSAYS
EIRSVEMMKQ RGGKVWFIGP EFVDTGVTLA DTWYQMKPYT DTALILGMLY HAIDTTFDAD
GNKKTGGLLD VDYIDTMVYG FFDSPEYWIE TNYTKGTDTA VGTDINENAG KIYIDQTTAK
SEIDKWDKET GPFTIGRNTY PYRWKNKADT SLYVYQEPIV KVNAVPAGRS LSAYIMGSDA
RLTKAAYSGN YVADQFASKQ AKRNGSICSY ISSAGNTTKY KTKKDFLKPK NTKWASDITG
IPEQAIKDLA ELYFNQDNHP IYSEWCGAQQ KQANGVINMF ALQALLILSK SWGQTGDGLG
RAFGGARSNA AGTLNVSISR PDVPSSPATP VISCTQWHNA IKFAFKEQLT ANGYSAKYIP
DWDYRNSESG VYYEDGGAKA LYTWDREADG TIKTNADGYY KWKTGKDGKP LKAGFRFILN
SGGNIPMNQH MDPNDAREMF EALDLGSTQP DNPDTFCMVS FDNFLSPSPR WSDYVLPAAT
TWEQEDIISI SLGNSLYIPV VSNAPGQAKS QWNFTNDLLK AVGKLKGVGN ELATKFTGGI
PNQQIEDLVK DAFGKASVNP QSLYHGKTWE DFINNPYAPK TASEYAPVTV TKTTLRENLD
NYLAGNMSQA FISGIKTNEK TGYGAQWLQS TIDLCPKASG RFHVYSDSLV YCYEHRFEQW
HGYLASKGQA TGQANKDFEN DPLVYPIPLY YAYEDYFNEA YGVMNGKNTL DMSKGYLLTT
THDRYRAHSS QSENPYLREL THRIKGGALY SGNDWNEYGN IGAVQEVKAG ETANLARLNQ
TISNGQPIAG KENVASWSEV WMNNQDAAAE GIADGQLITI GNPIGDVRVI ARVTDRVVRG
FIGLHQGCWY DPDPVDGIDD GGCANTLMAQ RPSRVDHGNG QQSAMVWIKN K
//
