ID A0A2S0UCR8_9BACL Unreviewed; 978 AA.
AC A0A2S0UCR8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:AWB45615.1};
GN ORFNames=DCC85_16375 {ECO:0000313|EMBL:AWB45615.1};
OS Paenibacillus sp. CAA11.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1532905 {ECO:0000313|EMBL:AWB45615.1, ECO:0000313|Proteomes:UP000244407};
RN [1] {ECO:0000313|EMBL:AWB45615.1, ECO:0000313|Proteomes:UP000244407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAA11 {ECO:0000313|EMBL:AWB45615.1,
RC ECO:0000313|Proteomes:UP000244407};
RA Um Y., Kim S., Gong G.;
RT "Complete genome of CAA11.";
RL Submitted (APR-2018) 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; CP028922; AWB45615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0UCR8; -.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000244407; Chromosome.
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:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 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; 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; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 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.
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:UP000244407};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 4..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 80..120
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 142..169
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 185..214
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 261..317
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 978 AA; 108760 MW; 585B2236F3C327D5 CRC64;
MNEQSIKISV NGENYEAKQG MSVLEVINLA EIAHPQICHV PEVDPIQTCD TCIVEINGQL
KRACSTPAAE GMRISTNSEA AKAAQTEGMD RLLENHMLYC TVCDNNNGNC KLHNTVEMME
IEHQKYPYRP KVSPAEVDMS HPFYRYDPNQ CIACGQCVEV CQNLQVNETL SIDWEADIPR
VIWDQGSAIN DSSCVSCGQC VTICPCNALM EKSMLGEAGF MSGVGEEVLE PMIDIVKAVE
PGYSGVFAIS EIEAAMRDTR TRKTKTVCTF CGVGCSFEVW TKGRKILKVQ PSHDAPVNAI
STCVKGKFGW DFVNSDQRLT TPLIRQGDAF VEATWDEALS LVAERLGSIK KEYGSDKIGF
ISSSKITNEE NYVIQKLARQ VFETNNIDNC SRYCQSPASD GLMSTVGIGG DSGTIKDIAS
AGLVILVGCA PAEGHPVLAT RIKRAHKLHG QKLIVADLRK HEMAERSDLF IRPKQGTDFV
WLTAVTKYMI DQGWHDASFI TDHVNFFAEY EKVLEKYTLE FAEQETGLSR AELISIAEMI
RDADGTAICW GMGVTQNIAG SHTSAAISNL LLATGNYMRP GAGAYPLRGH NNVQGACDMG
TLPPWLPGYQ HVSDDEARKR FEEAYGTLIS PVPGKDNIRM LDDIELGEMK AMYLVGEDMA
WVDSNANHVH EVLSKLDFFV VQDVFLSTTA QFADVILPAA PSLEKEGTFS NTERRVQRLY
QVFEPLGESK PDWWITTQIA KHMGFDWGYT HPSEIFAEMA SLTPFFSGCS YDMLEDWGSF
LWGSASGEST PLLYTDGFYF PDKKARFSLV EYVPPVEYPA EFDLVLNNGR LLEHFHEGNL
TNKSQGINHK FPDVFVEVSP ELAKERGVED GSLVRLESPY GAIKLRALVT DRVRGHEVYV
PMHSNSHESA VNLLTGSAVD VRTHTPAYKQ TKVRMQILNV KGVNPLPQTN PRYKKRNPQN
GVEVQRKWNR QDFVSLVD
//