ID A0A1W6JYB1_9CREN Unreviewed; 973 AA.
AC A0A1W6JYB1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=B6F84_03955 {ECO:0000313|EMBL:ARM75266.1};
OS Acidianus manzaensis.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=282676 {ECO:0000313|EMBL:ARM75266.1, ECO:0000313|Proteomes:UP000193404};
RN [1] {ECO:0000313|EMBL:ARM75266.1, ECO:0000313|Proteomes:UP000193404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YN-25 {ECO:0000313|EMBL:ARM75266.1,
RC ECO:0000313|Proteomes:UP000193404};
RA Ma Y., Yang Y., Xia J.;
RT "Sulfur activation and transportation mechanism of thermophilic Archaea
RT Acidianus manzaensis YN-25.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455};
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; CP020477; ARM75266.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6JYB1; -.
DR STRING; 282676.B6F84_03955; -.
DR KEGG; aman:B6F84_03955; -.
DR OrthoDB; 23466at2157; -.
DR Proteomes; UP000193404; 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:UniProtKB-EC.
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; cd00207; fer2; 1.
DR CDD; cd00508; MopB_CT_Fdh-Nap-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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..76
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 76..115
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 133..162
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 176..205
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 252..309
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 973 AA; 109888 MW; AC2F83E764FFDF35 CRC64;
MITLKVNGVE YKAQEGQTIL QFLQSHGIYI PHVCYNSYLG PIRTCDTCVV EYNGKIVRAC
ETKIQENAII NTESERVKEA REKAFNVILR NHDLYCTLCD NNVDCELHEA VSKLGIYSQK
FLPKPYDVDD SNPFYVYDPK QCILCGRCVE ACQDIVVNEV IKIDWSLNPP RVVWSNGKPI
DYSSCVSCGT CVTVCPVNAL MEKTLLGKAG YFTGINPEVK EKLIEAAKAG EKNFAPFMLI
SDIDKTLRKS LIKKTKTVCP FCGVGCSYEI WTRNEREILK VEPKPESPAN GIATCIKGKF
GQNYVNSKDR ITKPLIKEGD HFREATWEEA IKLVASKLTQ IKEKYGPDSI GIIASCTSTN
EEAYLAQKFA RQVIGTNNID NCARYCQSPA TTGLIRTVGY GADSGSAEDL ACADLVILIG
TNTAEAHPVI AGKIKRWHKL YNKKLVVIDV RKHEMAERAD LFITPNVGTD IILINGIAKF
IIDNNWEDKN FIRDRTVGFD DYKKSLEPFT LDYVEKVTGV DKEKIITIAK WIHESKGVSI
AWAMGITQHQ DGSETSTAIS NLLLLTGNYG KPCCGAFPLR GHANVQGAGD VGALYNFLPG
YQSLSDEKVR KKFEEAWNCE LPKKPGISST DMVDAILDGR IHAMYIMGED KVLADADQTK
TRDAFTKLDF LVVQDMFMTE TAKYADVILP ASAPLEKEGT YVNTERRIQR LYKVMEPLGE
SKSDWEIIQM IARAMGYNWN YSHPSEIMKE ISSLAPIFEG VTYDRLEGFK SLQWPVKKDG
TDSPYLYKDS FPFPDGKARF YPTKVIEPQN LDENYDLYLI NGRMLEHFHW MRMTGKTEGI
KYKVPQTFLE MSPELAEKKG LKTGDEVIIE SRSGRIKTKV LVSNRVSGNK VFLSIHDDKD
MNINWLTLDN KDPTARTPAY KETPVRVEKI ESCTTCEPPL PRWNPRYAER TPQIGVKVED
KWKRKDYMKV IDQ
//
