ID J6LDW2_9RHOB Unreviewed; 724 AA.
AC J6LDW2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Anaerobic dehydrogenase {ECO:0000313|EMBL:EJW11353.1};
GN ORFNames=A33M_3249 {ECO:0000313|EMBL:EJW11353.1};
OS Rhodovulum sp. PH10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW11353.1, ECO:0000313|Proteomes:UP000002930};
RN [1] {ECO:0000313|EMBL:EJW11353.1, ECO:0000313|Proteomes:UP000002930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH10 {ECO:0000313|EMBL:EJW11353.1,
RC ECO:0000313|Proteomes:UP000002930};
RX PubMed=23105089; DOI=10.1128/JB.01695-12;
RA Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT India.";
RL J. Bacteriol. 194:6363-6363(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJW11353.1}.
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DR EMBL; AKZI01000063; EJW11353.1; -; Genomic_DNA.
DR RefSeq; WP_008387206.1; NZ_AKZI01000063.1.
DR AlphaFoldDB; J6LDW2; -.
DR STRING; 1187851.A33M_3249; -.
DR PATRIC; fig|1187851.3.peg.2422; -.
DR eggNOG; COG0243; Bacteria.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000002930; Unassembled WGS sequence.
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:InterPro.
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 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 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; PS00490; MOLYBDOPTERIN_PROK_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000002930}.
FT DOMAIN 25..81
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 724 AA; 79690 MW; 93AF6FA2EA83E9EF CRC64;
MTSPTRPDAR AALAAAKIPG PDTGIVIRKT LCSICEYKCL VDAHVKDGRL IKVEGSRGSP
INDGTLCSKG AASRQWVYNP DRLQTPLLRT GERGEGRFRP ISWDEALDRI AERLAGFKAE
SGPESVVFFA GYPKVMRPFL KRLTHGFGSP NYCTESSTCF VGANMGGYLN YGYMLGQQGG
AEIDTTRCIL NWSTNHFYSQ APLGNRTFDA LDRGTKLIDV GPMLSPPAER ADIHLRLRPG
TCGALALSMA HVIIEENLHD RAFVENWTHG FDDYREYASK FPPAVAEQIT GVPKEKIVAA
ARLYATTKPA AIVTSACTTI HHTNGVQNHR AITALIGLTG NFDRPGGNHP VPTSYYRPSG
LAHREHAFEQ VKPWSEMAPR VGQDRFPVWS RIIPQAQAMA LPEQILTGKP YPIRSVLAFG
LNHRMWPAPE VTKQALLALD FFVDVELFMT ETAKFADIVL PACSTLERNE FSISPSRHAI
WTEQAVPPVG QSRPDIDIIL DLAKRLVPED ELLAQGHAAC LEWIFQPAGL SIAELAAHPG
GMVLEGRPAT PYEKYKKNGF PTPTKKMEFS STILAELGFD ALPVYREPLQ SPVATPELAK
EYPLVFTTGT RLPMFIHART FRVPWLRKLH PEPTADINPV DAGARGITHM QWVEVSTPRG
ALRVRANVTE YVPPGVVNMI HGYPGADANE LIDPDYLDPV SGHPGYKSLL CEVWPHPDQE
GAAP
//