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 03-AUG-2022, entry version 130.
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-containing
RT aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and
RT formaldehyde ferredoxin oxidoreductase from Thermococcus 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; DOI=10.1093/genetics/152.4.1299;
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 P.
RT 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; DOI=10.1016/s0021-9258(18)98669-2;
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; DOI=10.1016/s0021-9258(19)38690-9;
RA Mukund S., Adams M.W.W.;
RT "Characterization of a novel tungsten-containing formaldehyde ferredoxin
RT oxidoreductase from the hyperthermophilic archaeon, Thermococcus litoralis.
RT 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 ferredoxin
RT oxidoreductase.";
RL Science 267:1463-1469(1995).
CC -!- FUNCTION: Catalyzes the oxidation of aldehydes to their corresponding
CC carboxylic acids. May have a pyroglycolytic (saccharolytic) role.
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 -!- 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); Xref=ChEBI:CHEBI:60537;
CC Note=Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD)
CC cofactor per subunit.;
CC -!- ACTIVITY 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 aldehydes
CC 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}.
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DR EMBL; X79777; CAA56170.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80470.1; -; Genomic_DNA.
DR RefSeq; WP_011011461.1; NC_018092.1.
DR PDB; 1AOR; X-ray; 2.30 A; A/B=1-605.
DR PDBsum; 1AOR; -.
DR AlphaFoldDB; Q51739; -.
DR SMR; Q51739; -.
DR STRING; 186497.PF0346; -.
DR PRIDE; Q51739; -.
DR EnsemblBacteria; AAL80470; AAL80470; PF0346.
DR GeneID; 41712141; -.
DR KEGG; pfu:PF0346; -.
DR PATRIC; fig|186497.12.peg.360; -.
DR eggNOG; arCOG00706; Archaea.
DR HOGENOM; CLU_020364_1_0_2; -.
DR OMA; AYPISHE; -.
DR OrthoDB; 9593at2157; -.
DR PhylomeDB; Q51739; -.
DR BioCyc; MetaCyc:MON-21297; -.
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; -; 1.
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; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Reference proteome; Tungsten.
FT CHAIN 1..605
FT /note="Tungsten-containing aldehyde ferredoxin
FT oxidoreductase"
FT /id="PRO_0000064606"
FT BINDING 288
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 291
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 295
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 494
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1AOR"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1AOR"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1AOR"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:1AOR"
FT TURN 135..139
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1AOR"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 214..230
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:1AOR"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:1AOR"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 344..359
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 380..390
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 403..409
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 433..441
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:1AOR"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 472..491
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 503..514
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 520..541
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 545..548
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 553..557
FT /evidence="ECO:0007829|PDB:1AOR"
FT TURN 564..567
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 572..583
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 593..599
FT /evidence="ECO:0007829|PDB:1AOR"
FT HELIX 602..604
FT /evidence="ECO:0007829|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
