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Tungsten-containing aldehyde ferredoxin oxidoreductase (EC 1.2.7.5)

 AOR_PYRFU               Reviewed;         605 AA.
Q51739;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 114.
RecName: Full=Tungsten-containing aldehyde ferredoxin oxidoreductase;
EC=1.2.7.5;
Name=aor; OrderedLocusNames=PF0346;
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Pyrococcus.
NCBI_TaxID=186497;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
PubMed=7642512; DOI=10.1128/jb.177.16.4817-4819.1995;
Kletzin A., Mukund S., Kelley-Crouse T.L., Chan M.K.S., Rees D.C.,
Adams M.W.W.;
"Molecular characterization of the genes encoding the tungsten-
containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus
and formaldehyde ferredoxin oxidoreductase from Thermococcus
litoralis.";
J. Bacteriol. 177:4817-4819(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
PubMed=10430560;
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
DiRuggiero J., Robb F.T.;
"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and
P. horikoshii inferred from complete genomic sequences.";
Genetics 152:1299-1305(1999).
[3]
CHARACTERIZATION.
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
PubMed=1907273;
Mukund S., Adams M.W.W.;
"The novel tungsten-iron-sulfur protein of the hyperthermophilic
archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin
oxidoreductase. Evidence for its participation in a unique glycolytic
pathway.";
J. Biol. Chem. 266:14208-14216(1991).
[4]
PROTEIN SEQUENCE OF 1-26, BIOPHYSICOCHEMICAL PROPERTIES, AND
CHARACTERIZATION.
PubMed=8390467;
Mukund S., Adams M.W.W.;
"Characterization of a novel tungsten-containing formaldehyde
ferredoxin oxidoreductase from the hyperthermophilic archaeon,
Thermococcus litoralis. A role for tungsten in peptide catabolism.";
J. Biol. Chem. 268:13592-13600(1993).
[5]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
PubMed=7878465; DOI=10.1126/science.7878465;
Chan M.K.S., Mukund S., Kletzin A., Adams M.W.W., Rees D.C.;
"Structure of a hyperthermophilic tungstopterin enzyme, aldehyde
ferredoxin oxidoreductase.";
Science 267:1463-1469(1995).
-!- FUNCTION: Catalyzes the oxidation of aldehydes to their
corresponding carboxylic acids. May have a pyroglycolytic
(saccharolytic) role.
-!- CATALYTIC ACTIVITY: An aldehyde + H(2)O + 2 oxidized ferredoxin =
a carboxylate + 2 H(+) + 2 reduced ferredoxin.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Note=Binds 1 [4Fe-4S] cluster per subunit.;
-!- COFACTOR:
Name=W-bis(molybdopterin guanine dinucleotide);
Xref=ChEBI:CHEBI:60537;
Note=Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD)
cofactor per subunit.;
-!- ACTIVITY REGULATION: Inhibited by arsenite, iodoacetate and
cyanide.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.72 mM for formaldehyde {ECO:0000269|PubMed:8390467};
Vmax=295 umol/min/mg enzyme with formaldehyde as substrate
{ECO:0000269|PubMed:8390467};
Note=Significant activity only with aliphatic and aromatic
aldehydes and only at low concentration (0.5 mM).;
pH dependence:
Optimum pH is above 10. {ECO:0000269|PubMed:8390467};
Temperature dependence:
Optimum temperature is above 90 degrees Celsius.
{ECO:0000269|PubMed:8390467};
-!- SUBUNIT: Homodimer.
-!- MISCELLANEOUS: A significant amount of formaldehyde ferredoxin
oxidoreductase activity has been observed.
-!- SIMILARITY: Belongs to the AOR/FOR family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X79777; CAA56170.1; -; Genomic_DNA.
EMBL; AE009950; AAL80470.1; -; Genomic_DNA.
RefSeq; WP_011011461.1; NC_003413.1.
PDB; 1AOR; X-ray; 2.30 A; A/B=1-605.
PDBsum; 1AOR; -.
ProteinModelPortal; Q51739; -.
SMR; Q51739; -.
STRING; 186497.PF0346; -.
PRIDE; Q51739; -.
EnsemblBacteria; AAL80470; AAL80470; PF0346.
GeneID; 1468181; -.
KEGG; pfu:PF0346; -.
PATRIC; fig|186497.12.peg.360; -.
eggNOG; arCOG00706; Archaea.
eggNOG; COG2414; LUCA.
HOGENOM; HOG000014651; -.
KO; K03738; -.
OMA; ERIWNME; -.
OrthoDB; POG093Z03Y8; -.
BRENDA; 1.2.7.5; 5243.
SABIO-RK; Q51739; -.
EvolutionaryTrace; Q51739; -.
Proteomes; UP000001013; Chromosome.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0033726; F:aldehyde ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
Gene3D; 1.10.569.10; -; 1.
Gene3D; 1.10.599.10; -; 2.
Gene3D; 3.60.9.10; -; 1.
InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
InterPro; IPR013985; Ald_Fedxn_OxRdtase_dom3.
InterPro; IPR013983; Ald_Fedxn_OxRdtase_N.
InterPro; IPR036503; Ald_Fedxn_OxRdtase_N_sf.
InterPro; IPR001203; OxRdtase_Ald_Fedxn_C.
InterPro; IPR036021; Tungsten_al_ferr_oxy-like_C.
Pfam; PF01314; AFOR_C; 1.
Pfam; PF02730; AFOR_N; 1.
SMART; SM00790; AFOR_N; 1.
SUPFAM; SSF48310; SSF48310; 1.
SUPFAM; SSF56228; SSF56228; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing;
Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome;
Tungsten.
CHAIN 1 605 Tungsten-containing aldehyde ferredoxin
oxidoreductase.
/FTId=PRO_0000064606.
METAL 288 288 Iron-sulfur (4Fe-4S).
METAL 291 291 Iron-sulfur (4Fe-4S).
METAL 295 295 Iron-sulfur (4Fe-4S).
METAL 494 494 Iron-sulfur (4Fe-4S).
STRAND 6 12 {ECO:0000244|PDB:1AOR}.
TURN 13 16 {ECO:0000244|PDB:1AOR}.
STRAND 17 22 {ECO:0000244|PDB:1AOR}.
HELIX 25 31 {ECO:0000244|PDB:1AOR}.
HELIX 35 45 {ECO:0000244|PDB:1AOR}.
STRAND 59 63 {ECO:0000244|PDB:1AOR}.
TURN 65 68 {ECO:0000244|PDB:1AOR}.
STRAND 69 71 {ECO:0000244|PDB:1AOR}.
STRAND 77 82 {ECO:0000244|PDB:1AOR}.
TURN 84 86 {ECO:0000244|PDB:1AOR}.
STRAND 87 94 {ECO:0000244|PDB:1AOR}.
HELIX 98 104 {ECO:0000244|PDB:1AOR}.
STRAND 108 114 {ECO:0000244|PDB:1AOR}.
STRAND 120 125 {ECO:0000244|PDB:1AOR}.
STRAND 128 133 {ECO:0000244|PDB:1AOR}.
TURN 135 139 {ECO:0000244|PDB:1AOR}.
HELIX 142 153 {ECO:0000244|PDB:1AOR}.
STRAND 159 162 {ECO:0000244|PDB:1AOR}.
HELIX 165 168 {ECO:0000244|PDB:1AOR}.
STRAND 176 178 {ECO:0000244|PDB:1AOR}.
TURN 179 181 {ECO:0000244|PDB:1AOR}.
STRAND 182 184 {ECO:0000244|PDB:1AOR}.
STRAND 186 188 {ECO:0000244|PDB:1AOR}.
HELIX 189 195 {ECO:0000244|PDB:1AOR}.
STRAND 198 204 {ECO:0000244|PDB:1AOR}.
HELIX 214 230 {ECO:0000244|PDB:1AOR}.
HELIX 232 235 {ECO:0000244|PDB:1AOR}.
HELIX 237 241 {ECO:0000244|PDB:1AOR}.
HELIX 243 245 {ECO:0000244|PDB:1AOR}.
HELIX 246 252 {ECO:0000244|PDB:1AOR}.
TURN 259 262 {ECO:0000244|PDB:1AOR}.
HELIX 269 272 {ECO:0000244|PDB:1AOR}.
HELIX 274 280 {ECO:0000244|PDB:1AOR}.
STRAND 282 286 {ECO:0000244|PDB:1AOR}.
STRAND 296 301 {ECO:0000244|PDB:1AOR}.
TURN 302 304 {ECO:0000244|PDB:1AOR}.
STRAND 305 308 {ECO:0000244|PDB:1AOR}.
HELIX 312 318 {ECO:0000244|PDB:1AOR}.
HELIX 320 322 {ECO:0000244|PDB:1AOR}.
HELIX 327 340 {ECO:0000244|PDB:1AOR}.
HELIX 344 359 {ECO:0000244|PDB:1AOR}.
HELIX 365 368 {ECO:0000244|PDB:1AOR}.
HELIX 380 390 {ECO:0000244|PDB:1AOR}.
HELIX 396 399 {ECO:0000244|PDB:1AOR}.
HELIX 403 409 {ECO:0000244|PDB:1AOR}.
HELIX 413 415 {ECO:0000244|PDB:1AOR}.
HELIX 429 431 {ECO:0000244|PDB:1AOR}.
HELIX 433 441 {ECO:0000244|PDB:1AOR}.
HELIX 449 451 {ECO:0000244|PDB:1AOR}.
HELIX 454 457 {ECO:0000244|PDB:1AOR}.
STRAND 461 463 {ECO:0000244|PDB:1AOR}.
HELIX 472 491 {ECO:0000244|PDB:1AOR}.
HELIX 495 498 {ECO:0000244|PDB:1AOR}.
HELIX 503 514 {ECO:0000244|PDB:1AOR}.
HELIX 520 541 {ECO:0000244|PDB:1AOR}.
HELIX 545 548 {ECO:0000244|PDB:1AOR}.
HELIX 553 557 {ECO:0000244|PDB:1AOR}.
TURN 564 567 {ECO:0000244|PDB:1AOR}.
HELIX 572 583 {ECO:0000244|PDB:1AOR}.
HELIX 593 599 {ECO:0000244|PDB:1AOR}.
HELIX 602 604 {ECO:0000244|PDB:1AOR}.
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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