ID A0A1M6ETH7_9FIRM Unreviewed; 898 AA.
AC A0A1M6ETH7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=NAD-dependent formate dehydrogenase catalytic subunit {ECO:0000313|EMBL:SHI88713.1};
GN ORFNames=SAMN02745691_00997 {ECO:0000313|EMBL:SHI88713.1};
OS Parasporobacterium paucivorans DSM 15970.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Parasporobacterium.
OX NCBI_TaxID=1122934 {ECO:0000313|EMBL:SHI88713.1, ECO:0000313|Proteomes:UP000184342};
RN [1] {ECO:0000313|EMBL:SHI88713.1, ECO:0000313|Proteomes:UP000184342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15970 {ECO:0000313|EMBL:SHI88713.1,
RC ECO:0000313|Proteomes:UP000184342};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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DR EMBL; FQYT01000008; SHI88713.1; -; Genomic_DNA.
DR RefSeq; WP_073993259.1; NZ_FQYT01000008.1.
DR AlphaFoldDB; A0A1M6ETH7; -.
DR STRING; 1122934.SAMN02745691_00997; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000184342; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02790; MopB_CT_Formate-Dh_H; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041925; CT_Formate-Dh_H.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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 Reference proteome {ECO:0000313|Proteomes:UP000184342};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 2..82
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 82..121
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 141..171
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 184..212
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 222..277
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 898 AA; 99049 MW; 6DF85C42693B481F CRC64;
MKNVNIEIDG IKVTVPEETT ILKAAESIGI EIPTLCYLKD LTPDGSCRMC VVEVKGGRKK
GLFTACSEHC AEGMQVETRS EAVIDSRRFI LDMLMSIHEK RCLTCRQNSH CQLQELCMEY
GVEDTTYPGD APRFDVDTSN PFFDFDPNAC IMCRKCERVC TSLQGRKVIS INGRGIGTHM
SMVYDIKWSE SNCESCGNCV ANCPTGALLD KKIKGIPRLW DVKKVGTTCP HCGVGCQYNL
IVKDDEIIGT EALEGPSNRG MLCVKGRYGS FEFVKHPDRI KYPLIKRNGE FQRASWDEAL
DLIAAKILQH KKESGPDAIA GFSCSRSTNE DNYVFQKMMR AAIGTNNVDN CARLCHGPSV
VGLATTLGSG AMTNSIADIM EAPEVIFLIG SNTTEAHPVI GIQIRQAVLR GAKLIVADPR
AIDLMDYTYM HMQIRPGTNV AFANGIMNVI ISNGLEDQDY IAGRTEGYEE LKDLVKEYTP
EKVAQICGID KEMLIEAALM YAKADRAPII YCLGVTEHST GTEGVMSMSN MALLVGKLGK
YGCGVNPLRG QNNVQGACDM GCLPGDFPGY QKTSNPDNVS KFEKAWGCTL STTQGLRSTE
VFPAILEDRI KALYIFGEDP AATDPDSNHI RKALEKLDFL VVQELFMTET AKYADVILPG
ASYAQKEGTF TNTERRVQRV RKAVELEGEM RLDSDVFCDV MTRIGYPAHF DSAADIMREV
ASVTPSFAGV SHERLDGGES LQWPCTSSTD KGTCILHMDE FTRGRGLFKA IEFKEPDELP
DAEYPLTMIT GRMLYHYNNA SMTGRTEGIV QISNESYVEI NAQDAEKMNI RDGEKVKICS
RRGEVITSAR IGNVVSPNEV FMTFHFADGN VNEITNSVTD ELSGIPEYKV CAVKIEKA
//
