ID Q39S18_GEOMG Unreviewed; 671 AA.
AC Q39S18;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Molybdopterin-binding iron-sulfur cluster-binding oxidoreductase MopB-3 {ECO:0000313|EMBL:ABB32956.1};
GN OrderedLocusNames=Gmet_2738 {ECO:0000313|EMBL:ABB32956.1};
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB32956.1, ECO:0000313|Proteomes:UP000007073};
RN [1] {ECO:0000313|EMBL:ABB32956.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABB32956.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RX PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT "The genome sequence of Geobacter metallireducens: features of metabolism,
RT physiology and regulation common and dissimilar to Geobacter
RT sulfurreducens.";
RL BMC Microbiol. 9:109-109(2009).
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; CP000148; ABB32956.1; -; Genomic_DNA.
DR RefSeq; WP_004511721.1; NC_007517.1.
DR AlphaFoldDB; Q39S18; -.
DR STRING; 269799.Gmet_2738; -.
DR KEGG; gme:Gmet_2738; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_7; -.
DR Proteomes; UP000007073; Chromosome.
DR GO; GO:0051536; F:iron-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; cd02766; MopB_3; 1.
DR CDD; cd02786; MopB_CT_3; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 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; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR037920; YoaE_C.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007073}.
FT DOMAIN 3..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 671 AA; 73636 MW; 20FADA2485189EC1 CRC64;
MPTEIRRSVC PYDCPDTCGL LVEVEDGRAM RVSGDPEHPF TRGTLCPKML HYEKTAHSPL
RLTTPLVRIG PKGKGEFRAA TWNEAVAIIA ARWREIISGY GAEAILPYSY AGTMGLVHRN
CGHAFFHRLG ASRLDRTICS PAKEAGWKAI MGDTPSPHPD EVAESDLVIL WGINAAATNI
HFLHGVRETR KRGAQVWLID TYETPTAAAA DRVILSRPGS DGALALGMMH VIAREGLIDK
AFVEERIQGF AELAEQILPG YPPERVSAIT GVPASVIEDM ARCYARAQAP FIRLGSGLSR
YGNGAMTVRT ICALPALVGA YGKRGGGLLA STSTGAAFAM KEVTREDFML RPTRIVNMNR
LGHALTELSD PPVKSLYVYH SNPASVTPDQ NAILRGLARN DLFTVVHDRF MTDTARWADV
VLPACSSLET GDVYRAYGTY CIQRAWPAIP PVGESRSNWD TFAFLAEAMG FDEPYFSQTE
EEIIEHLVAI PAPMRDGIDL ARFEEGKGVE LPLAPDAPRT FRTPSGKVEI LNHREPEPLP
RHLPTHEEEG NLPLMLMTAP TLYALNASFY EQDELRERQG GMRLMVNPVE AGTRGIGDGE
RVIACNERGK VEFTLAVTDR VPPGVAVAEG VWWSEHAPGD RTVNALTSQR LTDRGNGSTF
YDTRIEVKKA R
//
