ID F7V8S9_CLOSS Unreviewed; 866 AA.
AC F7V8S9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Anaerobic dehydrogenase {ECO:0000313|EMBL:BAK46539.1};
GN Name=BisC {ECO:0000313|EMBL:BAK46539.1};
GN OrderedLocusNames=CXIVA_05720 {ECO:0000313|EMBL:BAK46539.1};
OS Clostridium sp. (strain SY8519).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK46539.1, ECO:0000313|Proteomes:UP000008937};
RN [1] {ECO:0000313|Proteomes:UP000008937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX PubMed=21914882; DOI=10.1128/JB.05637-11;
RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT "Complete genomic sequence of the O-desmethylangolensin-producing bacterium
RT Clostridium rRNA cluster XIVa strain SY8519, isolated from adult human
RT intestine.";
RL J. Bacteriol. 193:5568-5569(2011).
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; AP012212; BAK46539.1; -; Genomic_DNA.
DR RefSeq; WP_013976523.1; NC_015737.1.
DR AlphaFoldDB; F7V8S9; -.
DR STRING; 1042156.CXIVA_05720; -.
DR KEGG; cls:CXIVA_05720; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000008937; 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:InterPro.
DR Gene3D; 2.20.25.340; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR InterPro; IPR049032; AhtL-like_N.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR Pfam; PF21423; AhtL-like_1st; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008937}.
FT DOMAIN 14..68
FT /note="Pyrogallol hydroxytransferase large subunit-like N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF21423"
FT DOMAIN 74..590
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 750..846
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 866 AA; 98472 MW; B6E76C272985E7D9 CRC64;
MKGEIRLTNS STGGPVFVYV KDGKIVRITP MDFDETDPEG WTIKARGREF KAPRYTTIAP
FTAGQKSMIY SDRRILYPMK RVDFDPDGER NIQNRGISGY ERISWDEATD IVVKEINRIK
RESGPASIMS TPSSHHLWGN VGYRHSTYFR FMNLMGFTYA DHNPDSWEGW HWGGMHMWGF
SWRLGCPEQY DLLEDGLKYA EMIVFWSSDP EVNSGIYAAY ESHIRRRWLD ELGVKMVFID
PFFNHSANMW GMKWFSPKVG TDHAISFAIA YTWLTEGTYD KEYVKTHAYG FEEWAEYVLG
NGEDGIPKTC EWAEKESGVP ACEIRALARE WAKKNTYLAA GGMGGWGGAC RATHGIEWTR
GMIALATMQG LGKPGSNIWS TTQGVPTDYE FYFPGYAEGG ISGDCANSAA GFKFAWRMFD
GKTTFPAPVK VNWEAGQHIP RLKIPECIMN GKFEWYGKGF CGPTIEAQMH PYQYPAPGYG
KIKMYWKYGG PHIGTMTGTN RYAKMYTSES LEFVVSQSIW FEGEVPFADV ILPACTNYER
WDISEFANCS GYIPDNFQMA NNRVISLQAK CIEPLGESKS DYEIYALMAK KLGIYDIFTE
GKDELAWVEQ YYNATDCPKV MPWEEFFKKG YLVVPDNPNR KKTPALRWFA EDRVRDTPDW
GPAPNQTVGL KGLQTTTGKV EFISTSLKRF EEQGFVDEYR PSMHKYVPAW ESWHAEVAKK
YPLGMLSPHP RFSMHTMGDA KDSFMLDIKD HRVLVDGWYY WIIRMNTVDA EARGIKDGDL
VRAFNDRGSV ILCAQVGERV QPGTVHSYES SAEYAPLGKP GCSADRGGCV NILTPDRYMS
KYACGMAPNS AQVEVEKWDG GIYEIY
//
