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Database: UniProt
Entry: C7N1I9_SLAHD
LinkDB: C7N1I9_SLAHD
Original site: C7N1I9_SLAHD 
ID   C7N1I9_SLAHD            Unreviewed;       806 AA.
AC   C7N1I9;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing {ECO:0000313|EMBL:ACV21281.1};
GN   OrderedLocusNames=Shel_02110 {ECO:0000313|EMBL:ACV21281.1};
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:ACV21281.1, ECO:0000313|Proteomes:UP000002026};
RN   [1] {ECO:0000313|EMBL:ACV21281.1, 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   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP001684; ACV21281.1; -; Genomic_DNA.
DR   RefSeq; WP_012797392.1; NC_013165.1.
DR   AlphaFoldDB; C7N1I9; -.
DR   STRING; 471855.Shel_02110; -.
DR   KEGG; shi:Shel_02110; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_11; -.
DR   Proteomes; UP000002026; Chromosome.
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; 3.40.50.740; -; 2.
DR   Gene3D; 2.20.25.90; ADC-like domains; 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; 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; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
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}.
FT   DOMAIN          110..589
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          686..779
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   806 AA;  87620 MW;  EBEBF05F42F134C5 CRC64;
     MSGEKTVNPG ITRRGFMKGA AALGALGVTA GGIATATSSL APTNAQAESE EHVAYTYHQS
     HCGNMCALAC TVRDGRLVCI EPNSAMAERR YKTMCLKGVS EVQHIYSDKR IQTPLKRVGE
     RGAGEFEAVS WEEALDDIVS QIKDIQQSFG KDSVLVTTCA ECDVPFLATI LEARTCANNN
     GIDIGTGNGL DPATGMGWGF AMSAQEPRDW VNSRLVLNVG NNFCESSLAN ARVMFDAKDA
     GAHVVTVDPH FSTTACKSDE WIPIEVGTDA ALFLGMTTHI LDNNLGDQEF MAKHTSLPFL
     IDTKTGMLVR SEEGIVDEAA KAEAEAAGTE YMPFYPFLVI DEDGQKKPYT EAANPQLTVE
     GTFDGQQLVS VYSKLCESQK AYPTSWAAEV TGISQERIEA LAEEYAAGPS SLCVGWGGSD
     KLSNADITGH AAAVLVAVTG NIGKPGAGVG VYVGAQYAGY AAGFGEWAIP EKYGLMPGPA
     DLQMRELRQT DIVHAIVAVG DLLAQKVGNM KLTEEWTKTI DLIVTADVYF TEGAKWADYV
     LPLTSRFEYD AEVGNVKNGY NHICLQEKVL DPLFEAKTDL WFQRELAKRL GYEDALPETA
     DERVAAIMAG CTENVTLEQL KENQGVWPIT GIENPRLVAT DYAFYTESGN MEVYYQNLVD
     FNQALPQWEE NIEAYPGNPE REKYPLQLTN TRTRFRIHNQ FNDSAWLAQY YTPTVHVNPV
     DLEAQGIKTG DTVRLFNDRG EIKVAVAANE AIRPGSARLY EATTADYTVA GNMQDLTNDT
     PIERGAALMM GPVAPFSDTI VGIEKA
//
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