ID F7NDK0_9FIRM Unreviewed; 667 AA.
AC F7NDK0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:EGO65862.1};
GN ORFNames=ALO_00535 {ECO:0000313|EMBL:EGO65862.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO65862.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO65862.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO65862.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(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}.
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:EGO65862.1}.
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DR EMBL; AFGF01000007; EGO65862.1; -; Genomic_DNA.
DR RefSeq; WP_004573021.1; NZ_AFGF01000007.1.
DR AlphaFoldDB; F7NDK0; -.
DR STRING; 1009370.ALO_00535; -.
DR eggNOG; COG0243; Bacteria.
DR OrthoDB; 219031at2; -.
DR Proteomes; UP000003240; 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 CDD; cd02766; MopB_3; 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 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:UP000003240}.
FT DOMAIN 2..59
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 667 AA; 73425 MW; 48C7DD25CC2C6AB1 CRC64;
MVTVKRSVCP YDCPDACGLL VEVEAGSAVK VTGDPDHPYT RGSLCPKMNH YEKTVHSPGR
LTQPLLRAGA KGQGQFRPIS WEEAIRRIGG QWRTIIAEYG AEAILPYSYA GTMGLVQRHA
GHPFFHRLGA SRLERTICSP AKDYGWKAVM GSTLALHPDE APKSDFIILW GTNILATSIH
FFQIVRKAKQ QGAKVWLIDT YETPTAVAAD RVILVKPGSD GALALSMMQV MVREGWVDKD
FIARHVHGFE QFKDTLPAYA PEAVSDVTGL DPAVIVELAK TYASARAPFI SLGSGLSRYA
NGAMTVRCIT CLPALAGAWQ KSGGGLLSSI STGSAFAMEQ VTREDFMAEE TRIINMNQIG
DALTEAANPP VRSFYVYTSN PAAVAPDQNK VIAGLMRQDL FTVVHERFMT DTCLYADIVL
PAASSLETSD IYRSYGHYCL QRTYPAIPAV GESKSNWEVF QLLAREMGFE DAFFRQSADE
MIDSLLADPK PWMAGVDMDR LKNGLTVELP LPEGYKLDYR TPSGRIEILN EKEKEPLPRY
FPPAGESAPF WLMTAPNLYS LNSSFNERDD LLMQKEAMYL QMNPADAAAK QLTDRQQVVA
FNIRGEVPFI LKVTDKVPAG VVVADSIYWI KDAPGDRTVN ALTSQRLADR AAGSTFYDTK
VDVKGAC
//
