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Database: UniProt
Entry: D7DAS2_STAHD
LinkDB: D7DAS2_STAHD
Original site: D7DAS2_STAHD 
ID   D7DAS2_STAHD            Unreviewed;       625 AA.
AC   D7DAS2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE            EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN   OrderedLocusNames=Shell_0125 {ECO:0000313|EMBL:ADI31269.1};
OS   Staphylothermus hellenicus (strain DSM 12710 / JCM 10830 / BK20S6-10-b1 /
OS   P8).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Staphylothermus.
OX   NCBI_TaxID=591019 {ECO:0000313|EMBL:ADI31269.1, ECO:0000313|Proteomes:UP000002573};
RN   [1] {ECO:0000313|Proteomes:UP000002573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC   {ECO:0000313|Proteomes:UP000002573};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Anderson I.J., Woyke T.;
RT   "Complete sequence of Staphylothermus hellenicus DSM 12710.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADI31269.1, ECO:0000313|Proteomes:UP000002573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC   {ECO:0000313|Proteomes:UP000002573};
RX   PubMed=22180806; DOI=10.4056/sigs.2054696;
RA   Anderson I., Wirth R., Lucas S., Copeland A., Lapidus A., Cheng J.F.,
RA   Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Pati A., Mikhailova N., Woyke T., Klenk H.P.,
RA   Kyrpides N., Ivanova N.;
RT   "Complete genome sequence of Staphylothermus hellenicus P8.";
RL   Stand. Genomic Sci. 5:12-20(2011).
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; CP002051; ADI31269.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7DAS2; -.
DR   STRING; 591019.Shell_0125; -.
DR   KEGG; shc:Shell_0125; -.
DR   eggNOG; arCOG00706; Archaea.
DR   HOGENOM; CLU_020364_1_0_2; -.
DR   Proteomes; UP000002573; 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   ECO:0000313|EMBL:ADI31269.1}.
FT   DOMAIN          1..212
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   625 AA;  68851 MW;  846719E1ABC61AE9 CRC64;
     MGRILRVNLW RNKYYIEPLP PETVLRSWLG GRGLGVYLAL KEIDPKADPL GPRNKAFVMT
     GPITGVAGIP EAGRWCSVTK SPLTDTIHDS QSGGKFGPEL KFAGFDAIIL EDISEKPVYL
     WIHDGKVEIR DATHLWGKDV HSTTDIIQEE LAAEIGRDEA KKVKVLAIGP AGENLVRFAA
     LMNDKYRAAG RGGHGAVWGS KKIKAIAVRG HMKPEIAKKE MFKEVVIKMV KKHRENPVTS
     EGLPKLGTAI LVNIINKAGM LPTRNFRTGV FEGAEKISGE VLAEKYLDKK KSVEESCWGC
     VITCGRYTKV GKSPFSGEGG GPEYETIWAF GAQTGTDDLE AINKANYLCN ELGLDTISMG
     NTIGALMELV ELGKIPPEKL RGLNVKWGSP DAIVELVWRT AYRSGIGDEL AEGSWRLAQK
     YGAPEVSMSV RGQELPAYDP RGAQGQGLAY ATSNRGGCHV RAYLISPEVL GVPKLVDRFT
     TKGKPALVKE FQDVTAVVDS MIVCLFSSFA IWDEDYAEII SAVTGWDVSK DEVHKIGERI
     YNAERAFNVL SFGDGREYDT LPKRLLEEPM PEGPSKGHVV RLNEMLDEYY KLRGWIDGRP
     TRAKLEELGL KWVADRLEEE GLLPG
//
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