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Database: UniProt
Entry: O30159_ARCFU
LinkDB: O30159_ARCFU
Original site: O30159_ARCFU 
ID   O30159_ARCFU            Unreviewed;       578 AA.
AC   O30159;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE            EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN   OrderedLocusNames=AF_0077 {ECO:0000313|EMBL:AAB91151.1};
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325 {ECO:0000313|EMBL:AAB91151.1, ECO:0000313|Proteomes:UP000002199};
RN   [1] {ECO:0000313|EMBL:AAB91151.1, ECO:0000313|Proteomes:UP000002199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16
RC   {ECO:0000313|Proteomes:UP000002199};
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.P., Clayton R.A., Tomb J., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B., Peterson S.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L., Utterback T., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB91151.1; -; Genomic_DNA.
DR   PIR; E69259; E69259.
DR   RefSeq; WP_010877591.1; NC_000917.1.
DR   AlphaFoldDB; O30159; -.
DR   STRING; 224325.AF_0077; -.
DR   PaxDb; 224325-AF_0077; -.
DR   EnsemblBacteria; AAB91151; AAB91151; AF_0077.
DR   GeneID; 24793631; -.
DR   KEGG; afu:AF_0077; -.
DR   eggNOG; arCOG00706; Archaea.
DR   HOGENOM; CLU_020364_1_0_2; -.
DR   OrthoDB; 30771at2157; -.
DR   PhylomeDB; O30159; -.
DR   Proteomes; UP000002199; 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:SF8; 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:UP000002199}.
FT   DOMAIN          1..204
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   578 AA;  64716 MW;  A4B99B5FAB8AACC5 CRC64;
     MRDVVLVIDL NNYTYEVEHR PELFEKWLGG TGVAVQLMRE HMDPKADPLS PENVIVFATG
     PLTPAYPLAS KTVAMFKSPL TGNLGESHAG GRTAVSIAAA GYGAIVIKGA SKKPVYLVVE
     PGKVHFRDGR VLWGIPDSLI VGRILAENES GRGTRTMMRI GGAGERLVRY SCVTTETYRH
     FGRLGLGAVF GSKKLKALIV RGRKKYLPAD GKKYREVYDE IYRMAIESDA MKKYHLLGTA
     ANVIPLNELN ALPTKNLKAA RFEKAEEISG EALAEHNLGR RIACSHCPVA CIHLAALRLP
     YENEPYFFRT IMISYDYELI YSLGSMLGIG RRDDLLRLIH RVETYGLDAM STGVCLAWAT
     EALERGIITE RETLVKLNFG DVESYLKAID YIYEQPTEFY KHLAMGVQHA SEIYGGREFA
     LAFGGNEMPG YHTGYAAVLG YLTGMRHSHL DSAGYSLDQK VKDLSPEEVI NRLIEEESWR
     QVLSSLVVCF FARGIYTPEV ISRAFEPLGY SISPDELKNL GTEIYREKAR LKVAMGFNPK
     KLSVPKRIFE TPSLHGKLSE EFMARALDYY RKRLEEML
//
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