ID A0A5B8S8Z1_9SPHN Unreviewed; 947 AA.
AC A0A5B8S8Z1;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:QEA17047.1};
GN ORFNames=FRF71_13410 {ECO:0000313|EMBL:QEA17047.1};
OS Novosphingobium ginsenosidimutans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1176536 {ECO:0000313|EMBL:QEA17047.1, ECO:0000313|Proteomes:UP000321172};
RN [1] {ECO:0000313|EMBL:QEA17047.1, ECO:0000313|Proteomes:UP000321172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW-6 {ECO:0000313|EMBL:QEA17047.1,
RC ECO:0000313|Proteomes:UP000321172};
RX PubMed=23568197; DOI=.4014/jmb.1212.12053;
RA Kim J.K., He D., Liu Q.M., Park H.Y., Jung M.S., Yoon M.H., Kim S.C.,
RA Im W.T.;
RT "Novosphingobium ginsenosidimutans sp. nov., with the ability to convert
RT ginsenoside.";
RL J. Microbiol. Biotechnol. 23:444-450(2013).
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: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404}.
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; CP042345; QEA17047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B8S8Z1; -.
DR KEGG; ngf:FRF71_13410; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000321172; Chromosome.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0045333; P:cellular respiration; IEA:UniProt.
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:UP000321172}.
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 202..231
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 238..294
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 920..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 103095 MW; FF97E32B3F371622 CRC64;
MGYERQVDFG TPAVQSDSAV SLTIDGRSVT VPAGTSIMRA AAESGGSIPS LCATDSVKAF
GSCRMCLVQI EGRRGTPASC TTPVEPGMVV HTQTALLTRL RRGVMELYIS DHPLDCLTCS
ANNDCELQDT AAEVGLRDVR YGYAGENHLG LETDASNPYF DFDPSKCIAC SRCVRACDEV
QGTLALTMDG RGFASKISAG QAGDDFLSSE CVSCGACVQA CPTATLQEKA VKEIGKPERA
VITTCAYCGV GCTFRAEMRG EQLVRMVPWK DGKANRGHSC VKGRFAWGYA NHQDRITEPM
IRDSIEEPWR VVSWAEAFAH TAARLNAIKA QHGPRALGGI TSSRCTNEET FLVQKLVRAG
FGSNNVDTCA RVCHSPTGYG LKTTFGTSAG TQDFDSVMDS DVILVIGANP TDAHPVFASR
MKRRLRQGAK LIVIDPRRID LVRSPHIQAA HHLPLQPGTN VAVLTAMAHV IVTEGLADEA
FIRERCDWDE YQDWARFVSD EKHSPEVLEA VTRVPAAELR AAARLFATGG NGAIYYGLGV
TEHSQGSSTV MAIANLAMVT GNIGRRGVGV NPLRGQNNVQ GACDMGSFPH ELSGYRHISD
VATRGLFEQV WGVTLDPEPG LRIPNMLDAA LDGSFRAIYI QGEDILQSDP NTHHVAAGLK
AMELVIVHDL FLNETANYAH VFLPGSTFLE KNGTFTNAER RIQLVRKVME PANGLEDWEV
TQEIARAMGL EWNYAHPSEI MDEIARLTPT FAGVSFGRLD REGSLQWPVN DKAPDGSPIM
HVDGFVRGKG KFVVTDYVPT DEKTGPRFPL LLTTGRILSQ YNVGAQTRRT ANTVWHDEDL
LEIHPTDAEN RGIKSGDWVR LASRTGETTL RAEVTERVAP GVVYTTFHHP ATQANVVTTE
FSDWATNCPE YKVTAVQVSP SNGPTEWQES YASWSEKSRR IAAEPAE
//
