ID A7GVS4_CAMC5 Unreviewed; 816 AA.
AC A7GVS4;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Molybdopterin-containing oxidoreductase III, DMSO/TMAO/BSO reductase family, catalytic subunit {ECO:0000313|EMBL:EAU00844.1};
GN ORFNames=CCV52592_2044 {ECO:0000313|EMBL:EAU00844.1};
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105 {ECO:0000313|EMBL:EAU00844.1, 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}.
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; CP000767; EAU00844.1; -; Genomic_DNA.
DR RefSeq; WP_011991615.1; NC_009715.2.
DR AlphaFoldDB; A7GVS4; -.
DR STRING; 360105.CCV52592_2044; -.
DR KEGG; ccv:CCV52592_2044; -.
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 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; 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; 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:UP000006380}.
FT DOMAIN 81..551
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 671..790
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 816 AA; 91031 MW; EB72477EE42DD537 CRC64;
MKRRDFIKAS VLAASVAQAS RIDGITQTIF DNKKVFGANR FGLFWANTNS AQLVSVSDFE
GDKFPNTMNY SLPDSIQNEN RVLYPMVRKS YLKAGKPSKS ELRGKDEFVR VSWDTALDLA
AKALKENFDK YGAESIYGEC YWWGGSGKVS WGRTVAHRML KVLGGYVEES GDYSTGAGLV
IMPHVLGSSA VYDTPTKWKA IVKNAKNVVF WGTDPIVTNQ ISSIPPTHDC YIGMQDLKKA
GTKTFSVNVM TNDTARYYGS ETILVRPNTD TAMIIGMCHH LFTSGLYDAE FIKKYTVGFN
KFKAYFMGET DDKIVKDAAW ASKICGVPAE TIAKFAETIA KEPTTVLIGR ALQRADHGEQ
PFWALVVLNA MLGHIGKEGL GFEFSLGYNS SGGTDKIAPV LKGISTRISE KYENVGGAPW
KTTKNITIPS SRSIEALEHP GKEIDYDGTK IKLPHMRVAY MASGSIFTRH QDVNNIVKQW
RKFDTVITAE PYWTSTAKFS DIVLPVAIEV ERNDINQTGS TGEYIVAYKP VITPMGESRS
DYWICQQICK RWGREEVFTE GKDELGWMRE FYADAQEQAK NLSVSMPSFE EFYENGFVRF
EKDNTETELY TRLAAFRENP NKNRLGTPSG KIEIYSPTIA KFGYSDCPAH PTWLEPKEWL
GDAKKTAKYP LHIVSPHSRY RLHSQLNNSI IRNFAEVSGR EPILVNPADA KERGLATGDI
VRVFNDRGEI LAGVLVTDIV PPRVAAICEG AWYDPQNWGE KSLCQHGCVN VLTFDKGTSS
LAQSNSAHTA LAQIEKFKGE IRPLTAFSKP KILQSL
//
