ID E1STP9_FERBD Unreviewed; 820 AA.
AC E1STP9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family {ECO:0000313|EMBL:ADN76162.1};
GN OrderedLocusNames=Fbal_1959 {ECO:0000313|EMBL:ADN76162.1};
OS Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Ferrimonadaceae; Ferrimonas.
OX NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN76162.1, ECO:0000313|Proteomes:UP000006683};
RN [1] {ECO:0000313|EMBL:ADN76162.1, ECO:0000313|Proteomes:UP000006683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT
RC {ECO:0000313|Proteomes:UP000006683};
RX DOI=10.4056/sigs.1161239;
RA Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., Tice H.,
RA Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y., Jeffries C., Tapia R., Brettin T., Detter J., Han C.,
RA Yasawong M., Rohde M., Tindall B., Goker M., Woyke T., Bristow J.,
RA Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL Stand. Genomic Sci. 3:174-182(2010).
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; CP002209; ADN76162.1; -; Genomic_DNA.
DR RefSeq; WP_013345468.1; NC_014541.1.
DR AlphaFoldDB; E1STP9; -.
DR STRING; 550540.Fbal_1959; -.
DR GeneID; 67182170; -.
DR KEGG; fbl:Fbal_1959; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000006683; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR011888; Anaer_DMSO_reductase.
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 NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 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:UP000006683}.
FT DOMAIN 40..101
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 820 AA; 90175 MW; A720961BE4F79C12 CRC64;
MLRRDFLKLS ASAGAVTCLA ACGDDDNDNE PVAPPEVGDE AINFSACLVN CGSNCPLKVF
SKEGVITRIE TDHATTDQYG DHQVRACLRG RSMKQRTYAA DRLKAPMKRK AGSRRGSGQF
EEISWEQAFQ EIGQKVIELQ ANYGPRSIFH HYSSGAYYGF ASSACLQRAL RLSGGHLNYY
GNYSWATLNV ASPATFGTGG TSGTRLSEIR NSDLVVGFAF NPFEIRMSGS GEQIDFLNAI
EQRRQTGNLD VIIVDPRYTD SNLGKENQWL PIRPGTDGAL AEAVAYQMIS SGWVEQNSKA
FLDQYAIGYD RASLERAQSD NPDYATLINP EENYHDYIMG VGAYTLARTP DWAAAICGIP
SRLIVDLADK IMNAKSPYIT IGAGCNRQAC GEQTMRALYM LPILTGKLGQ NGVNNGELPT
NFGLSRSGMS AGANPESASI SFYTWAEAIE RGAEMTPTRD AVKGLGDGED KLGVNIKAVF
SSSGNAIINQ HSDINHTRQI LEDDSLCELI VVVDCWMTAS ARFADYILPD TTWVESNDLA
DDSYASGETG YLTFMSTGLE PLYNCRTLYQ IGLGLAQVFG KEQEYSEGRS EQEWLEYLYE
GTRASNPELN LPATYAEAQQ VGFFRRHSPD TYVALQDFVN GGEPLSTPSG KIEIYSLDWA
KKRAEWIPAS DQPYDQITPL PQYTAAWQGY EDEATRDDYP LQIVGYHTKG RVHSSYHNVE
WLREAVEDAA WFNPMDAARY GVTKGQMITL TSPRGAIRVR AKITPRVMPG VVAMAQGAWY
KANRIGEVDP GGCVNTLTLY HPTAVAKGNP QHTIRVKVTG
//
