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Database: UniProt/TrEMBL
Entry: A2BJR2_HYPBU
LinkDB: A2BJR2_HYPBU
Original site: A2BJR2_HYPBU 
ID   A2BJR2_HYPBU            Unreviewed;       611 AA.
AC   A2BJR2;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   28-JUN-2023, entry version 72.
DE   RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE            EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN   OrderedLocusNames=Hbut_0351 {ECO:0000313|EMBL:ABM80223.1};
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426 {ECO:0000313|EMBL:ABM80223.1, ECO:0000313|Proteomes:UP000002593};
RN   [1] {ECO:0000313|EMBL:ABM80223.1, ECO:0000313|Proteomes:UP000002593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5
RC   {ECO:0000313|Proteomes:UP000002593};
RX   PubMed=17350933;
RA   Brugger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
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; CP000493; ABM80223.1; -; Genomic_DNA.
DR   RefSeq; WP_011821541.1; NC_008818.1.
DR   AlphaFoldDB; A2BJR2; -.
DR   STRING; 415426.Hbut_0351; -.
DR   EnsemblBacteria; ABM80223; ABM80223; Hbut_0351.
DR   GeneID; 4782266; -.
DR   KEGG; hbu:Hbut_0351; -.
DR   eggNOG; arCOG00707; Archaea.
DR   HOGENOM; CLU_020364_1_0_2; -.
DR   OMA; AHHKDAW; -.
DR   OrthoDB; 30771at2157; -.
DR   Proteomes; UP000002593; 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:SF5; 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   ECO:0000313|EMBL:ABM80223.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002593}.
FT   DOMAIN          9..211
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   611 AA;  68018 MW;  0B3E29415CE8F326 CRC64;
     MASEKLFSWF KRILWVDLSR GEFREWRYPG EMARMFVGGR GYAIKILWDH LPEGADPLGP
     DNLLILAVGP LTGLPGPSTG KMVVAAKSPL TGGYGDGNIG TRAAVNLRAA GWDAVVIRGV
     ARKPSILVIE DDKAWLEPAD DLWGLDTFRA ADKLEERFGK TAGILLIGPG GENMVRYATI
     VSQKGRSGGR PGMGAVMGSK KLKAIVVRGT KKPELFHPEE ELRIGTEAIK FVKSSPNYEF
     WMRQGTMMTI EWSQNASVLP TYNFREGVFD GWEGISGNYM EKVKVTTKSC PLCPMSCGHV
     VKDAEGQPSE LDYENVAMLG SNIGISRLED AALLNRLADM YGIDTISLGN TLGYALEAAE
     RGKLELDATW GETRKLAKLV EDIAYRRGVG DLLAEGVKRV SEKVGETWYA MHVKGLEVSA
     YDCHAAPGMA LSYATSPIGA HHKDAWVISW EVQHGRFKYG REKVLRVIEL QRIRGGFFET
     AVTCRFPFVE LGLALDYYVK MFQAATGLSY SLEDHFTVAD RIYTLIRLFW VREHGGWGIE
     MDLPPERWFR EPLTKGPLKG AKLDKDKFIE MLKIYYRERG WAENGVPLPE TVKKLGLGED
     AVRLAERYSS K
//
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