ID J7IQV7_DESMD Unreviewed; 856 AA.
AC J7IQV7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing {ECO:0000313|EMBL:AFQ44015.1};
GN OrderedLocusNames=Desmer_2075 {ECO:0000313|EMBL:AFQ44015.1};
OS Desulfosporosinus meridiei (strain ATCC BAA-275 / DSM 13257 / KCTC 12902 /
OS NCIMB 13706 / S10).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=768704 {ECO:0000313|EMBL:AFQ44015.1, ECO:0000313|Proteomes:UP000005262};
RN [1] {ECO:0000313|EMBL:AFQ44015.1, ECO:0000313|Proteomes:UP000005262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC {ECO:0000313|Proteomes:UP000005262};
RX PubMed=23105050; DOI=10.1128/JB.01392-12;
RA Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA Ollivier B., Klenk H.P., Spring S., Loy A.;
RT "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT and Desulfosporosinus acidiphilus DSM22704T.";
RL J. Bacteriol. 194:6300-6301(2012).
RN [2] {ECO:0000313|Proteomes:UP000005262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-275 / DSM 13257 / NCIMB 13706 / S10
RC {ECO:0000313|Proteomes:UP000005262};
RA Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Tapia R., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Peters L., Pitluck S., Woyke T., Pester M., Spring S., Ollivier B.,
RA Rattei T., Klenk H.-P., Wagner M., Loy A.;
RT "Finished genome of Desulfosporosinus meridiei DSM 13257.";
RL Submitted (AUG-2012) 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP003629; AFQ44015.1; -; Genomic_DNA.
DR RefSeq; WP_014902929.1; NC_018515.1.
DR AlphaFoldDB; J7IQV7; -.
DR STRING; 768704.Desmer_2075; -.
DR KEGG; dmi:Desmer_2075; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_9; -.
DR OrthoDB; 219031at2; -.
DR Proteomes; UP000005262; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; 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 Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 2.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
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; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 47..106
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 856 AA; 96122 MW; 52373A7B3CEE4358 CRC64;
MGTQNLKLTR RHFLKLTAAT GVVAGTIGTA SVIRQAGAAP KQGDSKINYV RTTCSPNCTG
ACGMNALVED GQIKSIIQAA DYPEADYNPR GCLKGLSMTN LIYGPDRLQK PLILTGKPGS
GDFKEASWNE TLDYTAGRLK EIAEKYGPES IGVVFQVGGT GYVQKGAVSR LATLAGWTMH
HAYDQNGDLP MFWPMTFGVQ SEEIEPREWH NSRYVMVFGS NILATRIPDA HFLLEARNRG
AKIMVFDPNF SPTAAKADEW FSIKPSSDAA VALGLARVLI EETLYDSDFI KTFTDLPLLV
RVDNGKRLKA DEVKGLTKPS DIPAYREAYV AYNGQFRAVH PEKLDLPSDV VIEGEVDVTL
KTGETVKVKP AFQLLKECLS QYTPEEIEKT AGIPKDDLLR IAREMAGTKP LHVIYGAGNY
QWYHGDLKGR ALALLPVLTG NIGKPGAGIS TYAGQYRIRF KVAEWWVPEG KKQNWLPFLY
VLHGPTKTMK AKWPKNGIKA LIVGWGNPFD QHNMSNRLRE MVEKEDLEFV VTTDFQMTTS
CQYSHAVLPA VSWYEKTDLV ATPVHPYLQL QQRLVDPLYE GKPEFWIVRE LAKRLNPDFE
KYFYPDLEPN QAAEKVIELL LETGGPEVAG ITLEHLRKGP VRLKSEVPGG RQIPFYEQVQ
HKKPFPPVSL PAKLEQTAQF VKSGRIEFYK DEDLMLQAGE ALPVHKPPFE ESEYALNPLA
KEKYQFCYVT RNAIYRVHST HSNNVWMNEL QEGKPRVWLS PEDGQEKGIK EGDEVEIYND
RGKLTAYAII DPGVGRKQAV FEQGWWSRYL KGASYNSLTY PFIKPTHEIY FVPGMWSPNT
AWNECLCDVR KVGDSL
//
