ID B6YXN1_THEON Unreviewed; 605 AA.
AC B6YXN1;
DT 20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN OrderedLocusNames=TON_1354 {ECO:0000313|EMBL:ACJ16844.1};
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850 {ECO:0000313|EMBL:ACJ16844.1, ECO:0000313|Proteomes:UP000002727};
RN [1] {ECO:0000313|EMBL:ACJ16844.1, ECO:0000313|Proteomes:UP000002727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1 {ECO:0000313|EMBL:ACJ16844.1,
RC ECO:0000313|Proteomes:UP000002727};
RX PubMed=18790866; DOI=10.1128/JB.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.S., Kwon K.K., Kim H.T., Park C.J., Lee H.W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.J., Lee J.H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
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; CP000855; ACJ16844.1; -; Genomic_DNA.
DR RefSeq; WP_012572316.1; NC_011529.1.
DR AlphaFoldDB; B6YXN1; -.
DR STRING; 523850.TON_1354; -.
DR GeneID; 7018383; -.
DR KEGG; ton:TON_1354; -.
DR PATRIC; fig|523850.10.peg.1363; -.
DR eggNOG; arCOG00706; Archaea.
DR HOGENOM; CLU_020364_1_0_2; -.
DR OrthoDB; 30771at2157; -.
DR Proteomes; UP000002727; 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 Tungsten {ECO:0000256|ARBA:ARBA00023245}.
FT DOMAIN 4..207
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 605 AA; 67280 MW; 6E31B036693AEF61 CRC64;
MFAYWGRILR VNLSTGKISE EKFDEKFAQK WLGTRGFGIY YLLKEIDPTV DPFSPENKII
YATGPLTGTT APTGGRYMVI TKSPLTGYIA MANSGGFFGA ELKFAGWDAI IVEGKADHPV
YIYINDDQVE IRDASHLWGK LVSETEEKLR EEVGDKRVRI ASIGPAGENL VRFAAVMNDE
HRAAGRGGVG AVMGSKNLKA IVVRGHKRVE IADRAKFTSV VKEKIDKLRN DPVAGGGLPK
YGTAVLVNII NQNGLYPTRN FQDSQFEYAE EQSGEAMTAK YLIRNKPCYA CPIGCGRVNK
LPTVGVTEGP EYESIWALGA HLGINDLASI IEANHMIDEL GMDTISTGGT LATAMELFEK
GLIKPEDLGE EAPPFRWGNT EVLHYYIEKI ARREGFGDKL AEGGYRLAEM YNGTEYFMGV
KKQELPAYDP RGAEGHGLGY ATNNRGGGHI KQYMISPEIL GYPYKMDPHD ISDEKVKMVI
IFQDLTALID AAGLCVFTTF GLGADDYRDM LNAALGWDLT TEEYLKIGER IWNAERLFNL
KAGLDPLKED TLPKRLLEEP VKQGPNKGRV VRLKEMLPRY YALRGWTEDG RIPEEKLEEL
GLNEF
//
