ID A0A428WK54_9ACTN Unreviewed; 923 AA.
AC A0A428WK54;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:RSM43458.1};
GN ORFNames=DMB66_53410 {ECO:0000313|EMBL:RSM43458.1};
OS Actinoplanes sp. ATCC 53533.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1288362 {ECO:0000313|EMBL:RSM43458.1, ECO:0000313|Proteomes:UP000287606};
RN [1] {ECO:0000313|EMBL:RSM43458.1, ECO:0000313|Proteomes:UP000287606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53533 {ECO:0000313|EMBL:RSM43458.1,
RC ECO:0000313|Proteomes:UP000287606};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-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}.
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:RSM43458.1}.
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DR EMBL; QHHV01000280; RSM43458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428WK54; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000287606; Unassembled WGS sequence.
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; 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; 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.
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:UP000287606}.
FT DOMAIN 18..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 96..135
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 158..189
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 201..230
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 237..293
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 923 AA; 99517 MW; 8BE3FC13BF1EA208 CRC64;
MSLLKETDYG TPARPGPPAV TVEVDGLAVA VPEGTSVLRA AAQAGVPIPK LCATDNLAAF
GSCRLCLVEI DGRRGTPASC TTPVAEGMRV RTQSPHLEKL RRGVMELYIS DHPLDCLTCP
ANGDCELQDM AGVVGLREVR YGYAGANHLD APKDTSNPYF DFDAAKCIAC SRCVRACDEV
QGTFALTIAG RGFDSHVAAG AGGSFMESEC VSCGACVQAC PTSTLQERSV VDLGMPTRSV
VTTCAYCGVG CSFKAELRGT ELVRMVPHKD GGANEGHSCV KGRFAFGYAS HPDRILKPMV
RERITDEWRE VEWDEAIGTV ARGMRTIQNR YGPAAIGAIS SSRCTNEEVY TVQKMVRAAF
GNNNIDTCAR VCHSPTGYGL KQTFGESAGT QDFRSVAEAD VIVVIGANPT DGHPVFASRM
KRRLREGARL VVVDPRRIDL VRSPHIEAEH HLQLRPGSNV AVVNAMAHVA VTEGLVALSF
VRERCEGFDE WAAFIAAPEH SPEAVESITG VPAADLRAAA RLYAGARNGA IYYGLGVTEH
SQGSTMVMGM ANLAMACGNI GREGVGVNPL RGQNNVQGSC DMGSFPHELP GYRHVSDDAV
RGVFEKLWGG TLLGEPGLRI PNMFDAAIDG SFRGLFVHGE DIAQSDPNLR HVSAALAAME
LVVVQDLFLN ETAKFAHVFL PGASFLEKDG TFTNAERRIN RVRSVMTPPT GKHEWQIICE
IATAMGYPMS YRHPSEIMDE IASVTPTFAG VSFETLDKLG SVQWPCDAAA PEGTPVMHVD
EFTRGRGKFM ITAYVPTEER TTRRFPLVLT TGRILSQYNV GAQTRRTGNV AWHPEDLLEV
HPHDAEDRGI RDGDLVTLTS RVGETTLRAK IADRMPVGVV YTTFHHPVTG ANVVTTEHSD
WATNCPEYKV TAVQVGLSRV TAP
//
