ID A0A1E4L7N9_9PROT Unreviewed; 266 AA.
AC A0A1E4L7N9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=formylmethanofuran dehydrogenase {ECO:0000256|ARBA:ARBA00012692};
DE EC=1.2.7.12 {ECO:0000256|ARBA:ARBA00012692};
GN ORFNames=ABS92_01435 {ECO:0000313|EMBL:ODU50960.1};
OS Thiobacillus sp. SCN 63-374.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660149 {ECO:0000313|EMBL:ODU50960.1, ECO:0000313|Proteomes:UP000094238};
RN [1] {ECO:0000313|EMBL:ODU50960.1, ECO:0000313|Proteomes:UP000094238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin]
CC = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:19841, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57727,
CC ChEBI:CHEBI:58151; EC=1.2.7.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000989};
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10-
CC methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3.
CC {ECO:0000256|ARBA:ARBA00004830}.
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:ODU50960.1}.
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DR EMBL; MEFK01000009; ODU50960.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4L7N9; -.
DR Proteomes; UP000094238; Unassembled WGS sequence.
DR GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR InterPro; IPR017550; Formylmethanofuran_DH_suC.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR NCBIfam; TIGR03122; one_C_dehyd_C; 1.
DR PANTHER; PTHR39673; TUNGSTEN FORMYLMETHANOFURAN DEHYDROGENASE, SUBUNIT C (FWDC); 1.
DR PANTHER; PTHR39673:SF7; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT C; 1.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
PE 4: Predicted;
KW Methanogenesis {ECO:0000256|ARBA:ARBA00022994};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 81..204
FT /note="Glutamate synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01493"
SQ SEQUENCE 266 AA; 27496 MW; B362E6E019E8FE76 CRC64;
MTTLSLRAVP NGRVDMTGVL PETLAGRRAD DIGKQIIHLA GSPLMLGDLF EVDVDETDML
VVRTDSDRLD CLGKGMNTGC LRVEGPAGHY AAQGMRGGEL DIRGDAGDGA ANGMMGGLLR
IRGNAGDWLG AALIGDRTGM AGGVVAVEGD AGDRLGDRMR RGLILVRGQA GNACGARLLA
GTLVVAGGCG TQPGTGLRRG SLILGRRPEA IPLSFNDSGR VDLSYLGLLH RHAEGFLPGL
LSASTQAHRY MGDLAFGGKG EILVLV
//
