ID J1L5N7_9EURY Unreviewed; 591 AA.
AC J1L5N7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN ORFNames=Metli_2184 {ECO:0000313|EMBL:EJG08125.1};
OS Methanofollis liminatans DSM 4140.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanofollis.
OX NCBI_TaxID=28892 {ECO:0000313|EMBL:EJG08125.1};
RN [1] {ECO:0000313|EMBL:EJG08125.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4140 {ECO:0000313|EMBL:EJG08125.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Lu M., Detter J.C.,
RA Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schuler E., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Methanofollis liminatans DSM 4140.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a
CC carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:16421, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001714};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the AOR/FOR family.
CC {ECO:0000256|ARBA:ARBA00011032}.
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DR EMBL; CM001555; EJG08125.1; -; Genomic_DNA.
DR RefSeq; WP_004040378.1; NZ_CM001555.1.
DR AlphaFoldDB; J1L5N7; -.
DR STRING; 28892.Metli_2184; -.
DR PATRIC; fig|28892.9.peg.2359; -.
DR HOGENOM; CLU_020364_1_0_2; -.
DR OrthoDB; 30771at2157; -.
DR Proteomes; UP000005095; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0033726; F:aldehyde ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.569.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 2; 1.
DR Gene3D; 1.10.599.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 3; 1.
DR Gene3D; 3.60.9.10; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
DR InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
DR InterPro; IPR013985; Ald_Fedxn_OxRdtase_dom3.
DR InterPro; IPR013983; Ald_Fedxn_OxRdtase_N.
DR InterPro; IPR036503; Ald_Fedxn_OxRdtase_N_sf.
DR InterPro; IPR001203; OxRdtase_Ald_Fedxn_C.
DR InterPro; IPR036021; Tungsten_al_ferr_oxy-like_C.
DR PANTHER; PTHR30038; ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR PANTHER; PTHR30038:SF0; TUNGSTEN-CONTAINING ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR Pfam; PF01314; AFOR_C; 1.
DR Pfam; PF02730; AFOR_N; 1.
DR SMART; SM00790; AFOR_N; 1.
DR SUPFAM; SSF48310; Aldehyde ferredoxin oxidoreductase, C-terminal domains; 1.
DR SUPFAM; SSF56228; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
PE 3: Inferred from homology;
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 4..207
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 591 AA; 63294 MW; B60C001DB0F312BF CRC64;
MDGYAGKIVY ADLGGGTVEI GPTPDDLKRQ YLGGRGFGAR IVADRVDPTI DPLSPASVFV
LASGPLTGTG IPLGSRYEVS AKSPLNGTLA SANSGGTFGW KIKKAGFDAA VISGRSEKPV
YLFLNEGAAE LRDASPYWGK DVYETTASLL ADLGDPKAKV ACIGPAGEKQ SLLACIMNDD
DRAAGRNGFG AVMGSKNLKA FVATGNLPIG VADQERLNAV KERIREKIQK NGICEALTKY
GTSVLVNIVN ENGILPTRNF QSGHFAGAEG ISGERIAETI LKKNAGCYAC IVKCSRVCEI
DGEVHEGPEY EPVWAFGADI DNDDIKLVTK ASWECNRLGL DAIGTPGAIA CAMEMREKGF
IDEGPQFGEV DGLLDLVRQI GYREGFGAEL ADGSYRFAER HGHPELSMSV KKQDLPAYDP
RGLQGHGLSY ATSVRGGDHV YGYLIAPEVL GSPEKLDPYV SEGKAGWVKI FQDLTAAIDA
SGMCLFTSFA LDAQDYADLV TATTGMAMDA DALLRTGERI WNLQKVFNIG AGYTRSDDTL
PERLLTEPLQ DLAPKGRVWE PGRLLDEYYA LRGWDAEGVP TPEKLKELGL D
//
