ID Q5JEI3_THEKO Unreviewed; 633 AA.
AC Q5JEI3;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN OrderedLocusNames=TK0072 {ECO:0000313|EMBL:BAD84261.1};
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014 {ECO:0000313|EMBL:BAD84261.1, ECO:0000313|Proteomes:UP000000536};
RN [1] {ECO:0000313|EMBL:BAD84261.1, ECO:0000313|Proteomes:UP000000536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1
RC {ECO:0000313|Proteomes:UP000000536};
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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=W-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60537;
CC Evidence={ECO:0000256|ARBA:ARBA00001930};
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; AP006878; BAD84261.1; -; Genomic_DNA.
DR RefSeq; WP_011249027.1; NC_006624.1.
DR AlphaFoldDB; Q5JEI3; -.
DR STRING; 69014.TK0072; -.
DR EnsemblBacteria; BAD84261; BAD84261; TK0072.
DR GeneID; 78446575; -.
DR KEGG; tko:TK0072; -.
DR PATRIC; fig|69014.16.peg.74; -.
DR eggNOG; arCOG00706; Archaea.
DR HOGENOM; CLU_020364_1_0_2; -.
DR InParanoid; Q5JEI3; -.
DR OrthoDB; 30771at2157; -.
DR PhylomeDB; Q5JEI3; -.
DR Proteomes; UP000000536; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000536};
KW Tungsten {ECO:0000256|ARBA:ARBA00023245}.
FT DOMAIN 7..207
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 633 AA; 70306 MW; 70A6F5E2893509E0 CRC64;
MEAKGGYWGK ILRVNLTTKE VKVEPLPEEF PRKYLGGVGF GTRVLYEEVP KGADPLGPEN
KMIITPGLFV DTGIGTGSKT AFNFKSPLTG GYGRAMAGAE LGVQLKRAGY DMLIIEGQSE
EPVLLVINDD EVKIVPADAY WGLTTGEARS KAKEEYPGYA TAFIGPAGER LSLISIIETD
ERQAARGGPG AVLGSKKLKG ILVKGSKKVP IADPEKLREL IKKWALIFKD HPATKADMEY
GSGEFLDWMN RERGTFPVRN WQMGFFKKAY EKAKEEGREH IGIDPYFWAP KYRAGRRPCP
LCNKPCSQYV KVESKKWGTF MVDGPEYETL YSFGGVLEID DFETVAYLNY LADQYGLDTI
SAGVTIAWAM EAYERGLLTK EDTDGIELTF GNGEAAVEAL RKMAYREGNL GKLLADGVKR
ASERLGKESW KFAMHVKGME PPAYDVRGIK GMALAFAVSV RGADHLTAGA YGTELVGRWW
KFDGVDRTKG ENKGFEIAFH ENLMAIYDAT GTCKFSRHMY FLEGFPELIE AVTGMNIGEA
ELMVIGERIM NIARAFNVRE GFSRKDDTLP YRIMWEPIPE GVSKGLHVPP WELDRMLDEY
YQARGWSRDG IPTKAKLIAL DLPDIAEDIG AGI
//
