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Database: UniProt/SWISS-PROT
Entry: AOR_PYRFU
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Original site: AOR_PYRFU 
ID   AOR_PYRFU               Reviewed;         605 AA.
AC   Q51739;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   28-MAR-2018, entry version 113.
DE   RecName: Full=Tungsten-containing aldehyde ferredoxin oxidoreductase;
DE            EC=1.2.7.5;
GN   Name=aor; OrderedLocusNames=PF0346;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=7642512; DOI=10.1128/jb.177.16.4817-4819.1995;
RA   Kletzin A., Mukund S., Kelley-Crouse T.L., Chan M.K.S., Rees D.C.,
RA   Adams M.W.W.;
RT   "Molecular characterization of the genes encoding the tungsten-
RT   containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus
RT   and formaldehyde ferredoxin oxidoreductase from Thermococcus
RT   litoralis.";
RL   J. Bacteriol. 177:4817-4819(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and
RT   P. horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [3]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=1907273;
RA   Mukund S., Adams M.W.W.;
RT   "The novel tungsten-iron-sulfur protein of the hyperthermophilic
RT   archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin
RT   oxidoreductase. Evidence for its participation in a unique glycolytic
RT   pathway.";
RL   J. Biol. Chem. 266:14208-14216(1991).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-26, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   CHARACTERIZATION.
RX   PubMed=8390467;
RA   Mukund S., Adams M.W.W.;
RT   "Characterization of a novel tungsten-containing formaldehyde
RT   ferredoxin oxidoreductase from the hyperthermophilic archaeon,
RT   Thermococcus litoralis. A role for tungsten in peptide catabolism.";
RL   J. Biol. Chem. 268:13592-13600(1993).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=7878465; DOI=10.1126/science.7878465;
RA   Chan M.K.S., Mukund S., Kletzin A., Adams M.W.W., Rees D.C.;
RT   "Structure of a hyperthermophilic tungstopterin enzyme, aldehyde
RT   ferredoxin oxidoreductase.";
RL   Science 267:1463-1469(1995).
CC   -!- FUNCTION: Catalyzes the oxidation of aldehydes to their
CC       corresponding carboxylic acids. May have a pyroglycolytic
CC       (saccharolytic) role.
CC   -!- CATALYTIC ACTIVITY: An aldehyde + H(2)O + 2 oxidized ferredoxin =
CC       a carboxylate + 2 H(+) + 2 reduced ferredoxin.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC   -!- COFACTOR:
CC       Name=W-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60537;
CC       Note=Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD)
CC       cofactor per subunit.;
CC   -!- ENZYME REGULATION: Inhibited by arsenite, iodoacetate and cyanide.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.72 mM for formaldehyde {ECO:0000269|PubMed:8390467};
CC         Vmax=295 umol/min/mg enzyme with formaldehyde as substrate
CC         {ECO:0000269|PubMed:8390467};
CC         Note=Significant activity only with aliphatic and aromatic
CC         aldehydes and only at low concentration (0.5 mM).;
CC       pH dependence:
CC         Optimum pH is above 10. {ECO:0000269|PubMed:8390467};
CC       Temperature dependence:
CC         Optimum temperature is above 90 degrees Celsius.
CC         {ECO:0000269|PubMed:8390467};
CC   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: A significant amount of formaldehyde ferredoxin
CC       oxidoreductase activity has been observed.
CC   -!- SIMILARITY: Belongs to the AOR/FOR family. {ECO:0000305}.
DR   EMBL; X79777; CAA56170.1; -; Genomic_DNA.
DR   EMBL; AE009950; AAL80470.1; -; Genomic_DNA.
DR   RefSeq; WP_011011461.1; NC_003413.1.
DR   PDB; 1AOR; X-ray; 2.30 A; A/B=1-605.
DR   PDBsum; 1AOR; -.
DR   ProteinModelPortal; Q51739; -.
DR   SMR; Q51739; -.
DR   STRING; 186497.PF0346; -.
DR   PRIDE; Q51739; -.
DR   EnsemblBacteria; AAL80470; AAL80470; PF0346.
DR   GeneID; 1468181; -.
DR   KEGG; pfu:PF0346; -.
DR   PATRIC; fig|186497.12.peg.360; -.
DR   eggNOG; arCOG00706; Archaea.
DR   eggNOG; COG2414; LUCA.
DR   HOGENOM; HOG000014651; -.
DR   KO; K03738; -.
DR   OMA; ERIWNME; -.
DR   OrthoDB; POG093Z03Y8; -.
DR   BRENDA; 1.2.7.5; 5243.
DR   SABIO-RK; Q51739; -.
DR   EvolutionaryTrace; Q51739; -.
DR   Proteomes; UP000001013; 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; -; 1.
DR   Gene3D; 1.10.599.10; -; 2.
DR   Gene3D; 3.60.9.10; -; 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   Pfam; PF01314; AFOR_C; 1.
DR   Pfam; PF02730; AFOR_N; 1.
DR   SMART; SM00790; AFOR_N; 1.
DR   SUPFAM; SSF48310; SSF48310; 1.
DR   SUPFAM; SSF56228; SSF56228; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing;
KW   Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome;
KW   Tungsten.
FT   CHAIN         1    605       Tungsten-containing aldehyde ferredoxin
FT                                oxidoreductase.
FT                                /FTId=PRO_0000064606.
FT   METAL       288    288       Iron-sulfur (4Fe-4S).
FT   METAL       291    291       Iron-sulfur (4Fe-4S).
FT   METAL       295    295       Iron-sulfur (4Fe-4S).
FT   METAL       494    494       Iron-sulfur (4Fe-4S).
FT   STRAND        6     12       {ECO:0000244|PDB:1AOR}.
FT   TURN         13     16       {ECO:0000244|PDB:1AOR}.
FT   STRAND       17     22       {ECO:0000244|PDB:1AOR}.
FT   HELIX        25     31       {ECO:0000244|PDB:1AOR}.
FT   HELIX        35     45       {ECO:0000244|PDB:1AOR}.
FT   STRAND       59     63       {ECO:0000244|PDB:1AOR}.
FT   TURN         65     68       {ECO:0000244|PDB:1AOR}.
FT   STRAND       69     71       {ECO:0000244|PDB:1AOR}.
FT   STRAND       77     82       {ECO:0000244|PDB:1AOR}.
FT   TURN         84     86       {ECO:0000244|PDB:1AOR}.
FT   STRAND       87     94       {ECO:0000244|PDB:1AOR}.
FT   HELIX        98    104       {ECO:0000244|PDB:1AOR}.
FT   STRAND      108    114       {ECO:0000244|PDB:1AOR}.
FT   STRAND      120    125       {ECO:0000244|PDB:1AOR}.
FT   STRAND      128    133       {ECO:0000244|PDB:1AOR}.
FT   TURN        135    139       {ECO:0000244|PDB:1AOR}.
FT   HELIX       142    153       {ECO:0000244|PDB:1AOR}.
FT   STRAND      159    162       {ECO:0000244|PDB:1AOR}.
FT   HELIX       165    168       {ECO:0000244|PDB:1AOR}.
FT   STRAND      176    178       {ECO:0000244|PDB:1AOR}.
FT   TURN        179    181       {ECO:0000244|PDB:1AOR}.
FT   STRAND      182    184       {ECO:0000244|PDB:1AOR}.
FT   STRAND      186    188       {ECO:0000244|PDB:1AOR}.
FT   HELIX       189    195       {ECO:0000244|PDB:1AOR}.
FT   STRAND      198    204       {ECO:0000244|PDB:1AOR}.
FT   HELIX       214    230       {ECO:0000244|PDB:1AOR}.
FT   HELIX       232    235       {ECO:0000244|PDB:1AOR}.
FT   HELIX       237    241       {ECO:0000244|PDB:1AOR}.
FT   HELIX       243    245       {ECO:0000244|PDB:1AOR}.
FT   HELIX       246    252       {ECO:0000244|PDB:1AOR}.
FT   TURN        259    262       {ECO:0000244|PDB:1AOR}.
FT   HELIX       269    272       {ECO:0000244|PDB:1AOR}.
FT   HELIX       274    280       {ECO:0000244|PDB:1AOR}.
FT   STRAND      282    286       {ECO:0000244|PDB:1AOR}.
FT   STRAND      296    301       {ECO:0000244|PDB:1AOR}.
FT   TURN        302    304       {ECO:0000244|PDB:1AOR}.
FT   STRAND      305    308       {ECO:0000244|PDB:1AOR}.
FT   HELIX       312    318       {ECO:0000244|PDB:1AOR}.
FT   HELIX       320    322       {ECO:0000244|PDB:1AOR}.
FT   HELIX       327    340       {ECO:0000244|PDB:1AOR}.
FT   HELIX       344    359       {ECO:0000244|PDB:1AOR}.
FT   HELIX       365    368       {ECO:0000244|PDB:1AOR}.
FT   HELIX       380    390       {ECO:0000244|PDB:1AOR}.
FT   HELIX       396    399       {ECO:0000244|PDB:1AOR}.
FT   HELIX       403    409       {ECO:0000244|PDB:1AOR}.
FT   HELIX       413    415       {ECO:0000244|PDB:1AOR}.
FT   HELIX       429    431       {ECO:0000244|PDB:1AOR}.
FT   HELIX       433    441       {ECO:0000244|PDB:1AOR}.
FT   HELIX       449    451       {ECO:0000244|PDB:1AOR}.
FT   HELIX       454    457       {ECO:0000244|PDB:1AOR}.
FT   STRAND      461    463       {ECO:0000244|PDB:1AOR}.
FT   HELIX       472    491       {ECO:0000244|PDB:1AOR}.
FT   HELIX       495    498       {ECO:0000244|PDB:1AOR}.
FT   HELIX       503    514       {ECO:0000244|PDB:1AOR}.
FT   HELIX       520    541       {ECO:0000244|PDB:1AOR}.
FT   HELIX       545    548       {ECO:0000244|PDB:1AOR}.
FT   HELIX       553    557       {ECO:0000244|PDB:1AOR}.
FT   TURN        564    567       {ECO:0000244|PDB:1AOR}.
FT   HELIX       572    583       {ECO:0000244|PDB:1AOR}.
FT   HELIX       593    599       {ECO:0000244|PDB:1AOR}.
FT   HELIX       602    604       {ECO:0000244|PDB:1AOR}.
SQ   SEQUENCE   605 AA;  66631 MW;  86254EDF6756C00D CRC64;
     MYGNWGRFIR VNLSTGDIKV EEYDEELAKK WLGSRGLAIY LLLKEMDPTV DPLSPENKLI
     IAAGPLTGTS APTGGRYNVV TKSPLTGFIT MANSGGYFGA ELKFAGYDAI VVEGKAEKPV
     YIYIKDEHIE IRDASHIWGK KVSETEATIR KEVGSEKVKI ASIGPAGENL VKFAAIMNDG
     HRAAGRGGVG AVMGSKNLKA IAVEGSKTVP IADKQKFMLV VREKVNKLRN DPVAGGGLPK
     YGTAVLVNII NENGLYPVKN FQTGVYPYAY EQSGEAMAAK YLVRNKPCYA CPIGCGRVNR
     LPTVGETEGP EYESVWALGA NLGINDLASI IEANHMCDEL GLDTISTGGT LATAMELYEK
     GHIKDEELGD APPFRWGNTE VLHYYIEKIA KREGFGDKLA EGSYRLAESY GHPELSMTVK
     KLELPAYDPR GAEGHGLGYA TNNRGGCHIK NYMISPEILG YPYKMDPHDV SDDKIKMLIL
     FQDLTALIDS AGLCLFTTFG LGADDYRDLL NAALGWDFTT EDYLKIGERI WNAERLFNLK
     AGLDPARDDT LPKRFLEEPM PEGPNKGHTV RLKEMLPRYY KLRGWTEDGK IPKEKLEELG
     IAEFY
//
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