ID F6B9K3_DESCC Unreviewed; 1026 AA.
AC F6B9K3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:AEF94899.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:AEF94899.1};
DE Flags: Precursor;
GN OrderedLocusNames=Desca_2060 {ECO:0000313|EMBL:AEF94899.1};
OS Desulfotomaculum nigrificans (strain DSM 14880 / VKM B-2319 / CO-1-SRB)
OS (Desulfotomaculum carboxydivorans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=868595 {ECO:0000313|EMBL:AEF94899.1, ECO:0000313|Proteomes:UP000009226};
RN [1] {ECO:0000313|EMBL:AEF94899.1, ECO:0000313|Proteomes:UP000009226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC {ECO:0000313|Proteomes:UP000009226};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF94899.1, ECO:0000313|Proteomes:UP000009226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC {ECO:0000313|Proteomes:UP000009226};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL Submitted (MAY-2011) 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP002736; AEF94899.1; -; Genomic_DNA.
DR STRING; 868595.Desca_2060; -.
DR KEGG; dca:Desca_2060; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_0_9; -.
DR Proteomes; UP000009226; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
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:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 4.
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; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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 ECO:0000313|EMBL:AEF94899.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009226};
KW Selenium {ECO:0000313|EMBL:AEF94899.1};
KW Selenocysteine {ECO:0000313|EMBL:AEF94899.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1026
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003333481"
FT DOMAIN 47..104
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 804..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 204
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:AEF94899.1"
SQ SEQUENCE 1026 AA; 113853 MW; 8F9EAFDBE08E637A CRC64;
MRKISRRDFL KALSLGAGLT LVASPALASN SESKITGEKL PSKIRKVKET YTVCAFCGCG
CGIILYSDSN NKIVFCEGDP DHPINEGSLC SKGNAIIETY NVIDKKQGRI TNKLRVTKPL
YRAPGSTKWE EKSWDWVLSE IAKRVKKTRD ESFEEKDAKG VTVNRTTAIA TFGSASLDNE
ENYLLHKMFR SWGLINIEHH ARLUHSSTVA GLAASFGRGV MTNHFIDYKN SDVIMMIGSN
SAENHPQAMK WILKAKEKGG KLIVVDPRLN KSAGMADIHA RLRPGTDIAF INGMINYIIE
NNLYHKDYII NHTNASFLVN PDYKFEDGLF SGFTEKDGKK SYDTATWQYQ QDGDQIKKDP
TLQDPNCVFQ LLKKHVSRYD IKTVCQITGT PEETYRKVCE LFGSTGKPDK AGNVVYAMGI
TQHTHGTQNC RALCVLQLLL GNIGIAGGGV NAQRGESNVQ GSTDMAMLNH NLPGYIGMIY
ADKHPTLKDY LEKEVPKTSY WSNKGKFLIS MFKAWYGDKA TKENDFAYDW IPKHDGKNRS
HMGIFEQMSQ GKIKGMFAWG QNPAVGGPSS FQGRKALEKL DWLVAVDLFE TETAAFWHRP
EADPTQIKTE VFLLPAAMSY EKEGTVTNSG RWVQFRYKAV NPPGEAKSDL WIADRLFKAV
RKEYQNGGKF PDPILNMVWN YDKPGEDEPN IEQVALEING YDVATKQALP GFAKLADDGS
TACGCWILSG YWAMDKEAKT VAAKRRLLKD KSGLGLFPQF AFAWPANRRI VYNRCSADAA
GNPWNPQKAI IKWDPVKGNW DNADVPDFKA AEPAKDPNGK PTPIPPDKTQ SFFMNEEGYG
RLFAVKGVND GPLPEHYEPI ESPVKNILSK QQNMPLATRF KGDFSKVAET ASEKYPYIGT
THRVVEHYQS GAVTRSSPSL AEASAHMFAN ISPKLAQKIG VKTGDDVVIE TVRGQITCKV
AVSAVCLPLN VNGKEVEVIG MPWCFGYQGI ATGASANDLT PSVGDPNTNI PEYKAFLCNI
KKASKH
//
