ID A0A157SMD1_9BORD Unreviewed; 1147 AA.
AC A0A157SMD1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:SAI71474.1};
DE EC=1.8.5.3 {ECO:0000313|EMBL:SAI71474.1};
GN Name=dmsA {ECO:0000313|EMBL:SAI71474.1};
GN ORFNames=SAMEA3906487_02791 {ECO:0000313|EMBL:SAI71474.1};
OS Bordetella trematum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI71474.1, ECO:0000313|Proteomes:UP000076825};
RN [1] {ECO:0000313|EMBL:SAI71474.1, ECO:0000313|Proteomes:UP000076825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H044680328 {ECO:0000313|EMBL:SAI71474.1,
RC ECO:0000313|Proteomes:UP000076825};
RG Pathogen Informatics;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; LT546645; SAI71474.1; -; Genomic_DNA.
DR RefSeq; WP_063492093.1; NZ_UFUJ01000001.1.
DR AlphaFoldDB; A0A157SMD1; -.
DR STRING; 123899.SAMEA3906487_02791; -.
DR GeneID; 56589955; -.
DR KEGG; btrm:SAMEA390648702791; -.
DR PATRIC; fig|123899.6.peg.2778; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000076825; Chromosome 1.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
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:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR CDD; cd02759; MopB_Acetylene-hydratase; 1.
DR CDD; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR041930; Acetylene_hydratase.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:SAI71474.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076825}.
FT DOMAIN 2..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 800..916
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 1065..1147
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 1147 AA; 126100 MW; 62B4813A25E2302F CRC64;
MTEFKQGFCT LCRSRCGTIN EVQDDSLVAV RPDPSHPTGQ AMCMKGKSAP ELVHSPHRVL
YPMRRTRPKG DPDPGWVRIS WEEALGETAR RLGAIRAESG PEGVVFAVTT PSGTPLSDSI
DWIERFVRLF GSPNICYATE ICNWHKDFAH AFTFGCGMPP ADYAEAELIV LWGHNPANTW
LAQANALSQG RARGARMIVV DPRPTALARQ ADVWLPVRPG TDAALALGLM HLLITQARYD
TAFVHDWTNA PLLVRADSGD FLCERELWPQ AQHDRFVVWD DTLQAAVPYD TRQAAADQGG
GFRLRGEFRL MTESGAALIC HPVFELLARA CADYPPETVA HITGVPPQVL RQAADLFGSL
RRIAYHAWTG IGQHTNATQS ERAVATLYAL CGSFDRIGGN RVRLGPPVNA VNSLALLPRS
QRDKALGLQA RPIGPAAHGW VTAADTYRAI LHGQPYRVRA MMAFGTNLPV SQGDTAEAQQ
ALEQLEFHVH LDLFETPAAK YADILLPANT PWEREGLRVG FEINDRAAGW VQLRQRMVTP
RGESRSDNEV LFDLAVRLGM GEQFFHGSLE AGWNHMLAPL GLDVARLRQH PEGLACPVDA
AERKFARADD GGVHGFDTPT RRVEIYSERL LQHGQPALPT FVEPADSPRD PRATRQGRFP
YVLSSAKNGF YCHSQHRSLV SLRKRAPDPV VELSPALANA KGILEGDWVR LRTRVGAARF
VARLTPQLAD DVLVAEFGWW QGCSELDREA LTLQGAGGSN FNALISADRC DPVSGSVPHR
SFLCNVDLDP ATELRQRRWQ GYRAFRVSAL REEAEGVLGI HFEPLEETAL PDYRPGQHIE
LRLEQGEGGS LSRAYSLTGA AEVAGRRGYS IAVRHQRGRD ADGMPFEGRM SGALHRCLKV
GDRVMLRAPS GGWVVPRRSP QPLCLIAGGI GITPFVSLLE SLPDDAEGPE IWLYYANQNS
RTHAFRARIA QHRARLPHLH VRDFYTSPLP GDRPGIDFDD SRYIDASVID DVLIAQRARF
YMCGPPAMMD AVSAGLRARG VPRFDIFSEV FRSPPPPVAG GDQRFSVRFA RSRKEAAIWT
PGEGTLLTFA ESLGVQMAAG CRVGQCESCA VQLLAGKVRH LHGGEPEDPA DCLACQAVPT
DDIVIDA
//
