ID I3Y0T4_SULBS Unreviewed; 807 AA.
AC I3Y0T4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing {ECO:0000313|EMBL:AFL69808.1};
GN OrderedLocusNames=Sulba_2546 {ECO:0000313|EMBL:AFL69808.1};
OS Sulfurospirillum barnesii (strain ATCC 700032 / DSM 10660 / SES-3).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurospirillaceae; Sulfurospirillum.
OX NCBI_TaxID=760154 {ECO:0000313|EMBL:AFL69808.1, ECO:0000313|Proteomes:UP000006176};
RN [1] {ECO:0000313|EMBL:AFL69808.1, ECO:0000313|Proteomes:UP000006176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700032 / DSM 10660 / SES-3
RC {ECO:0000313|Proteomes:UP000006176};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Stolz J., Arkin A.,
RA Dehal P., Oremland R., Saltikov C., Basu P., Hollibaugh J., Newman D.,
RA Stolyar S., Hazen T., Woyke T.;
RT "Complete sequence of Sulfurospirillum barnesii SES-3.";
RL Submitted (JUN-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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP003333; AFL69808.1; -; Genomic_DNA.
DR RefSeq; WP_014770671.1; NC_018002.1.
DR AlphaFoldDB; I3Y0T4; -.
DR STRING; 760154.Sulba_2546; -.
DR KEGG; sba:Sulba_2546; -.
DR PATRIC; fig|760154.4.peg.2540; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_7; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000006176; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 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; cd02778; MopB_CT_Thiosulfate-R-like; 1.
DR CDD; cd02755; MopB_Thiosulfate-R-like; 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; IPR006311; TAT_signal.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 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.
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 43..99
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 807 AA; 91094 MW; DCE7466363CB1966 CRC64;
MKVEISRRRF LQGSVALSVV GGTALSSTSI LANSDKKPEN LLMKEVPTIC EMCVNKCAAI
AHVKNGIVTK LEPNPLFPKS RNMLCARGAA GIHAVYDPDR LKYPLIRAGE RGDGQYRRVS
WDEAYAYIQN KLVKILDEEE DNRSCIGYCA GEGLAEHTFK TFMADKFGSS NFLNHSTICL
QTAVSGYTLT IGGYGQADLE NAKYVIMAGA NRAEAILTPD TMDMFKRTRG RGMKLVVVDP
RYTNTAMHAD TYLPIRPGTD LAFVLALTYV AISTKSYNRT YVAKNFVDFD KYEKHILEGG
YTPEWAEKIT GISASEIRKI AHDFMAHAPQ SVYYQGRRTT WSKNDFQLRR AMALFTALGG
GIDVKGGIVF GKKLPLGDHA VSAPMYANAQ PRIDKNVAAV VGATGSWVGW RNMVAEGKTP
YPIRGMFVYK QNPMLSVPNS AKTRQMFEKM DLVVVIDTMP SDTAMLADVI LPECTYLERE
DPVQSFAGVE PAIILREKVI EPMYETKPVN DIMRELAQKL TQPLWEITKK YDEDVQEAIE
EEDEQSVFEE GGFDLAEPFM HSQEETNHHM VVSKYGEDAW KILREKGVFY PNMLTYFKKI
DNNTYEYYPK DKKFYSVLKL EEEYDPEAYL HDLCVNPTDI AELKRSFNTP NKKVECYLSS
MVARKIDPMP TWHDEEYVKV PEGKFKFITG RHAQFTQSST ANNIMLLELM RENYLWINDK
EAQKLGIRFG DNIEVTSSVG QVRIKAYPTP KIVPQTVFYI HGFGAKSDGL TFAHRNGASD
NEIIEDTIEP VHGCANMHDT LVTLRRV
//
