[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; PubMed=7642512 [NCBI, ExPASy, EBI, Israel, Japan] 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; Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.; "The complete sequence of the Pyrococcus furiosus genome."; Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[3]	CHARACTERIZATION. STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; PubMed=1907273 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: Catalyzes the oxidation of aldehydes to their corresponding carboxylic acids. May have a pyroglycolytic (saccharolytic) role.
CATALYTIC ACTIVITY: An aldehyde + H₂O + 2 oxidized ferredoxin = an acid + 2 H⁺ + 2 reduced ferredoxin.
COFACTOR: Binds 1 4Fe-4S cluster per subunit.
COFACTOR: Binds 1 tungstopterin cofactor per subunit.
ENZYME REGULATION: Inhibited by arsenite, iodoacetate and cyanide.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=0.72 mM for formaldehyde;
	V_max=295 µmol/min/mg enzyme with formaldehyde as substrate;
	Note=Significant activity only with aliphatic and aromatic aldehydes and only at low concentration (0.5 mM);
pH dependence:	Optimum pH is above 10;
Temperature dependence:	Optimum temperature is above 90 degrees Celsius;

SUBUNIT: Homodimer.
MISCELLANEOUS: A significant amount of formaldehyde ferredoxin oxidoreductase activity has been observed.
SIMILARITY: Belongs to the AOR/FOR family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X79777; CAA56170.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE010158; AAL80470.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_578075.1; -.

3D structure databases

PDB

1AOR; X-ray; 2.30 A; A/B=1-605.

[ExPASy / RCSB / EBI]

PDBsum

1AOR; -.

ModBase

Q51739.

Family and domain databases

InterPro

IPR013985; Ald_Fedxn_OxRdtase_3.
IPR013983; Ald_Fedxn_OxRdtase_N.
IPR001203; OxRdtase_Ald_Fedxn_C.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.599.10; Oxred_Ald_Fedxn_3; 1.
G3DSA:3.60.9.10; Oxred_Ald_Fedxn_N; 1.

Pfam

PF01314; AFOR_C; 1.
PF02730; AFOR_N; 1.
Pfam graphical view of domain structure.

SMART

SM00790; AFOR_N; 1.
SMART graphical view of domain structure.

BLOCKS

Q51739.

Genome annotation databases

1468181; -.

AE009950_GR; PF0346.

pfu:PF0346; -.

fig|186497.1.peg.352; -.

Phylogenomic databases

HOGENOM

Q51739; -.

Other

LinkHub

Q51739; -.

Genome annotation databases

CMR

Q51739; PF0346.

Other

ProtoNet

Q51739.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Tungsten.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 605`	`605`	`Tungsten-containing aldehyde ferredoxin oxidoreductase.`	`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`	`7`
`TURN`	`13 16`	`4`
`STRAND`	`17 22`	`6`
`HELIX`	`25 31`	`7`
`HELIX`	`35 45`	`11`
`STRAND`	`59 63`	`5`
`TURN`	`65 68`	`4`
`STRAND`	`69 71`	`3`
`STRAND`	`77 82`	`6`
`TURN`	`84 86`	`3`
`STRAND`	`87 94`	`8`
`HELIX`	`98 104`	`7`
`STRAND`	`108 114`	`7`
`STRAND`	`120 125`	`6`
`STRAND`	`128 133`	`6`
`TURN`	`135 139`	`5`
`HELIX`	`142 153`	`12`
`STRAND`	`159 162`	`4`
`HELIX`	`165 168`	`4`
`STRAND`	`176 178`	`3`
`TURN`	`179 181`	`3`
`STRAND`	`182 184`	`3`
`STRAND`	`186 188`	`3`
`HELIX`	`189 195`	`7`
`STRAND`	`198 204`	`7`
`HELIX`	`214 230`	`17`
`HELIX`	`232 235`	`4`
`HELIX`	`237 241`	`5`
`HELIX`	`243 245`	`3`
`HELIX`	`246 252`	`7`
`TURN`	`259 262`	`4`
`HELIX`	`269 272`	`4`
`HELIX`	`274 280`	`7`
`STRAND`	`282 286`	`5`
`STRAND`	`296 301`	`6`
`TURN`	`302 304`	`3`
`STRAND`	`305 308`	`4`
`HELIX`	`312 318`	`7`
`HELIX`	`320 322`	`3`
`HELIX`	`327 340`	`14`
`HELIX`	`344 359`	`16`
`HELIX`	`365 368`	`4`
`HELIX`	`380 390`	`11`
`HELIX`	`396 399`	`4`
`HELIX`	`403 409`	`7`
`HELIX`	`413 415`	`3`
`HELIX`	`429 431`	`3`
`HELIX`	`433 441`	`9`
`HELIX`	`449 451`	`3`
`HELIX`	`454 457`	`4`
`STRAND`	`461 463`	`3`
`HELIX`	`472 491`	`20`
`HELIX`	`495 498`	`4`
`HELIX`	`503 514`	`12`
`HELIX`	`520 541`	`22`
`HELIX`	`545 548`	`4`
`HELIX`	`553 557`	`5`
`TURN`	`564 567`	`4`
`HELIX`	`572 583`	`12`
`HELIX`	`593 599`	`7`
`HELIX`	`602 604`	`3`

Sequence information

Length: 605 AA [This is the length of the unprocessed precursor]

Molecular weight: 66631 Da [This is the MW of the unprocessed precursor]

CRC64: 86254EDF6756C00D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYGNWGRFIR VNLSTGDIKV EEYDEELAKK WLGSRGLAIY LLLKEMDPTV DPLSPENKLI 

        70         80         90        100        110        120 
IAAGPLTGTS APTGGRYNVV TKSPLTGFIT MANSGGYFGA ELKFAGYDAI VVEGKAEKPV 

       130        140        150        160        170        180 
YIYIKDEHIE IRDASHIWGK KVSETEATIR KEVGSEKVKI ASIGPAGENL VKFAAIMNDG 

       190        200        210        220        230        240 
HRAAGRGGVG AVMGSKNLKA IAVEGSKTVP IADKQKFMLV VREKVNKLRN DPVAGGGLPK 

       250        260        270        280        290        300 
YGTAVLVNII NENGLYPVKN FQTGVYPYAY EQSGEAMAAK YLVRNKPCYA CPIGCGRVNR 

       310        320        330        340        350        360 
LPTVGETEGP EYESVWALGA NLGINDLASI IEANHMCDEL GLDTISTGGT LATAMELYEK 

       370        380        390        400        410        420 
GHIKDEELGD APPFRWGNTE VLHYYIEKIA KREGFGDKLA EGSYRLAESY GHPELSMTVK 

       430        440        450        460        470        480 
KLELPAYDPR GAEGHGLGYA TNNRGGCHIK NYMISPEILG YPYKMDPHDV SDDKIKMLIL 

       490        500        510        520        530        540 
FQDLTALIDS AGLCLFTTFG LGADDYRDLL NAALGWDFTT EDYLKIGERI WNAERLFNLK 

       550        560        570        580        590        600 
AGLDPARDDT LPKRFLEEPM PEGPNKGHTV RLKEMLPRYY KLRGWTEDGK IPKEKLEELG 


IAEFY

Q51739 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools