ID   A7GYA3_CAMC5            Unreviewed;       839 AA.
AC   A7GYA3;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Molybdopterin-containing oxidoreductase II, DMSO/TMAO/BSO reductase family, catalytic subunit {ECO:0000313|EMBL:EAT99693.1};
GN   ORFNames=CCV52592_0394 {ECO:0000313|EMBL:EAT99693.1};
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105 {ECO:0000313|EMBL:EAT99693.1, ECO:0000313|Proteomes:UP000006380};
RN   [1] {ECO:0000313|Proteomes:UP000006380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
RL   Submitted (JUL-2007) 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; CP000767; EAT99693.1; -; Genomic_DNA.
DR   RefSeq; WP_009649906.1; NC_009715.2.
DR   AlphaFoldDB; A7GYA3; -.
DR   STRING; 360105.CCV52592_0394; -.
DR   GeneID; 61002188; -.
DR   KEGG; ccv:CCV52592_0394; -.
DR   HOGENOM; CLU_000422_13_3_7; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000006380; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006658; BisC.
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   NCBIfam; TIGR00509; bisC_fam; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006380}.
FT   DOMAIN          50..91
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          94..575
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          700..815
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   839 AA;  94571 MW;  6167564821BE3D06 CRC64;
     MNRQRRNILK YGAILGAMPI ASKFSAFSNL IGAQMSDIGS GLVRNGTVLT ATHWGMLNVT
     VKDGIIVKSE PYQKVSGIYN SLQYYTADSV YKTRIKYPMV RKSYLQNPNS PKPELRGRDE
     WVRVEYEDAI KLVARELKKT RKEHGDESIY AGSQGWKSSG NFHSSTILLH RFMNLTGGAI
     VTMGNYSTGA VSFTMPHVVG SIEVYEQQTS WPVVLENSKV VVIWGANPIL TLKIAWTTTD
     ELGFKYFEEL KSKDIEVVVI DPIRSETVKY YDKCKHIAPR PNTDVAMMLG MAHHLYISGK
     YDKDFIETYT YGFEKFLPYL LGKSDGVAKT PEWASKICQV KPEVIRELAD KFMDNRTMFI
     SGWSMQRAHH GEQPHWMLIT LASMIGQIGL PGGGFGLSYH YANGGVPTCK GGVITGISRG
     NIGNFDENGK FTGTHKSPAV QAWIEKTKKY NFPAPRIADV MLHPGKVIDH NGKKITYPDI
     QFFYWAGGNP MTHHQDLNTL TKAMQKPRTV VVNEIYWTPT AKMADIVFPI TTSFERNDIV
     MSGEYSNMHI VPMKQVVEKF AEAKDDYQVF SDLCKAYADG LYEVYTQNGK TEMDWIKEFY
     DAAYAQVKAV PDLSTDMKPF DEFWAENKPV IFASTPESDT YVRYGKFRED PILNVLGTPS
     GLIEIYSDVV AGFGYDDCWG HPAWFEPVEW LGMKDKPAEF HMISSHPEDR LHSQLNYTSL
     RDRYAINNRE PIWINKNVAK RKGIKDGDLV RVFNKRGEII AGAILTDDFG EDIVKINEGA
     WYDPDEKGCC KNGCPNVLTI DIPSSKLANG NIAHTALVNI EKFKGIAPEL TAFKDPKFA
//