ID C7N3M8_SLAHD Unreviewed; 979 AA.
AC C7N3M8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing {ECO:0000313|EMBL:ACV21619.1};
GN OrderedLocusNames=Shel_05600 {ECO:0000313|EMBL:ACV21619.1};
OS Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 /
OS RHS 1) (Peptococcus heliotrinreducens).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Slackia.
OX NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV21619.1, ECO:0000313|Proteomes:UP000002026};
RN [1] {ECO:0000313|EMBL:ACV21619.1, ECO:0000313|Proteomes:UP000002026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1
RC {ECO:0000313|Proteomes:UP000002026};
RX PubMed=21304663; DOI=10.4056/sigs.37633;
RA Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Lucas S.,
RA Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L., Kuske C.,
RA Brettin T., Detter J.C., Han C., Pitluck S., Pati A., Mavrommatis K.,
RA Ivanova N., Ovchinnikova G., Chen A., Palaniappan K., Schneider S.,
RA Rohde M., Chain P., D'haeseleer P., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT "Complete genome sequence of Slackia heliotrinireducens type strain (RHS
RT 1).";
RL Stand. Genomic Sci. 1:234-241(2009).
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; CP001684; ACV21619.1; -; Genomic_DNA.
DR RefSeq; WP_012797724.1; NC_013165.1.
DR AlphaFoldDB; C7N3M8; -.
DR STRING; 471855.Shel_05600; -.
DR KEGG; shi:Shel_05600; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_11; -.
DR Proteomes; UP000002026; 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:UniProtKB-KW.
DR CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 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; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 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; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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 Reference proteome {ECO:0000313|Proteomes:UP000002026};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..979
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038725402"
FT DOMAIN 64..120
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 979 AA; 108502 MW; 4486AAB4DF2A504D CRC64;
MTKSNLTRRS FIKAAGFTAA ASAIGASLAG CMQSDGGSAE GEGSADGNVK SSEGVTFSTH
IDYDTKLRTS CHGCIQMCPA IAYLKDGVVV KLEGDPEAPV SRGSLCIKGL NQVHTMYSPR
RVLHPLRHIE RGTNKWEQIS WDEAIDEAAQ HIADAINEYG PYSFFASVGG GGSYSFMEAM
TLPMALGSPT VFEPGCAQCY LPRWALSKLF YGGDDQSIAD NAVQEIFRPG DDNKAEVVVI
WGAQPSVSET AESGRGMAEL RAAGVKTIVV DPNFSPDAVH ADIWLPIRPA TDTKLILCWF
NYIFENKLYN EQFTKYWTNL PFLIDPDTKL PVKAQELFPD FEQTTPEHTP AYVCYDLKTN
AVAPFEYSAP ADSAVDPEIF WEGEFNGKTY KTAGQIYAEE AAPWTLEKTA EDCWLEADKI
EAAIRMYTHA DDGGPIDHVA GIANGVASDM TESASQVPIG LMGLDSIMGY INRPGATMTQ
KGGGYFTDAT GTQSLKRQYT FNNGFGGMFS AMYGIGAVIG LSDEQNEAWA RGEETPAGVA
DVSQQELANQ LLLDRIGMKD HKGLYAWCHS HIPSVREAIA TGEPFKPRVW FDMSGNKLAM
LGNAKSWYEV FPEVDYIITQ YPNITSFQFE AADLMFPLRE WLEEPMVNMT QLDTQWLQNE
CTHIGETVSH SIPAAQVLAK VAEKLGGDLP GLKPGYLGNP TEQANKDSVA ATLGAPSWDE
LIANTDQYVP HITEGYFNYN QHEVLAEDDD NLPIGFATES RKIETYCQIL LRTARTGYPY
CYPKPQEACD DYSPICVPIE PCESPYSEAE QQIADREEYP FVLTSGRVPY FHHGTMRHAA
YSRELFPCAE IRINPASAAE LGIEHMDWVK VTSRRGEIHA RAWLTEAINP HTVWMERFWN
PEAFDESQAN PDGGWRQMNV NVLTKNTAPF NEVFGSYTNR GFTVKIEKSE KPENVWVEPE
EFQPFMPTLQ GEARTEDVF
//
