Carbon monoxide dehydrogenase - Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)

Contribute

Read comments (?) or add your own

Q8TXX3 (COOS_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 61. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

to top of page

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

to top of page

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Carbon monoxide dehydrogenase
Short name=CODH
EC=1.2.99.2

Gene names

Name:	cooS
Ordered Locus Names:	MK0536

Organism

Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)

Taxonomic identifier

Taxonomic lineage

Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	CO + H₂O + A = CO₂ + AH₂.
Cofactor	Binds 3 4Fe-4S clusters per homodimer By similarity. Binds 2 nickel-iron-sulfur clusters per homodimer By similarity.
Subunit structure	Homodimer By similarity.
Domain	Cluster B is an all-cysteinyl-liganded 4Fe4S cluster; cluster C is a mixed Ni-Fe-S cluster which appears to be the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe4S cluster that bridges the two subunits of the CODH dimer By similarity.
Sequence similarities	Belongs to the Ni-containing carbon monoxide dehydrogenase family.
Caution	This protein lacks the conserved Cys in position 54; it is replaced by a Trp. It is therefore possible that the D-cluster is either altered or missing in this protein, which may not form homodimers.
Sequence caution	The sequence AAF86272.1 differs from that shown. Reason: Frameshift at positions 356, 372, 411 and 441.

Ontologies

Keywords
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Nickel
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	generation of precursor metabolites and energy Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC nickel cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

638

Carbon monoxide dehydrogenase

PRO_0000157144

Sites

Metal binding

1

Iron-sulfur 1 (4Fe-4S); shared with dimeric partner By similarity

Metal binding

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

1

Nickel-iron-sulfur By similarity

Metal binding

1

Nickel-iron-sulfur By similarity

Metal binding

1

Nickel-iron-sulfur By similarity

Metal binding

1

Nickel-iron-sulfur By similarity

Metal binding

1

Nickel-iron-sulfur By similarity

Metal binding

1

Nickel-iron-sulfur By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8TXX3 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B3A90308E67768C2
Show »

638

69,512

        10         20         30         40         50         60 
MEEKRSSCPY ADEAVCELVE HAKELNEEIP EIETPHIRWP VQFPKCPYGK QGVWCNICSN 

        70         80         90        100        110        120 
GPCRITEKTP RGVCGATADV IVARNFLRHV AAGAACYVHC LENAARALKS VADEESPYEI 

       130        140        150        160        170        180 
ADEKALRHAA EVYGLDTSGK PEDVAEEIAE FILEDIYRPR YEESEVFKAV VPDWRIEMYE 

       190        200        210        220        230        240 
EMGLIPGGAK SEIHDALVKT STNLNSDPVD MLLHVLRLGL ITGPVALFGV ETINDILFGS 

       250        260        270        280        290        300 
PKITQTEGGP GILDPDYVNI MTTGHQMALM KYLTDAAEKL EEEAKAAGAK GIRIIGATCV 

       310        320        330        340        350        360 
GDDFEARAEH LPDTYAGFAG NNFATEALAA TGLVDAIVSE FNCTFPGLKF YKEKLDVELV 

       370        380        390        400        410        420 
AVDDVAKVWG AELILWDPER AEEVAEEAVQ RAIEAFKERR SKHEDKIMEP KHRHENVVGF 

       430        440        450        460        470        480 
GYFSIEEAVG WENVLKLIEE GTIRGVCAIM GCTNLSSGGH NVPAVELAKE MIKRDVLVLG 

       490        500        510        520        530        540 
AGCVNGAFAN AGLFNPEAAE LAGDNLRQVC EELGIPPVLH YGPCLAIGKI EHLVFEIAEI 

       550        560        570        580        590        600 
LREKTGEEID IPDVPAVASA PQWLEEQALA DASSALALGI TLHVSPVPPV TGSELVTKTL 

       610        620        630 
LEDLPDLTGG ELIVETDMKR AGEILAEKIE EKRKRLGI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Random sequence analysis of the genomic DNA of Methanopyrus kandleri and molecular cloning of the gene encoding a homolog of the catalytic subunit of carbon monoxide dehydrogenase." Shin H.-S., Ryu J.-R., Han Y.-S., Choi Y.-J., Yu Y.G. J. Microbiol. Biotechnol. 9:404-413(1999) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens." Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A. Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF272857 Genomic DNA. Translation: AAF86272.1. Frameshift. AE009439 Genomic DNA. Translation: AAM01751.1.
RefSeq	NP_613821.1. NC_003551.1.
3D structure databases
ProteinModelPortal	Q8TXX3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1476637.
GenomeReviews	Gene locus MK0536 in contig AE009439_GR.
KEGG	mka:MK0536.
NMPDR	fig\|190192.1.peg.534.
Phylogenomic databases
HOGENOM	HBG393174.
OMA	CRITEKT.
ProtClustDB	CLSK862738.
Enzyme and pathway databases
BioCyc	MKAN190192:MK0536-MONOMER.
Family and domain databases
InterPro	IPR016101. CO_DH_a-bundle. IPR010047. CO_DH_cat. IPR004137. Prismane. IPR011254. Prismane-like. IPR016099. Prismane-like_a/b-sand. [Graphical view]
Gene3D	G3DSA:1.20.1270.30. CO_DH_a-bundle. 1 hit. G3DSA:3.40.50.2030. Prismane-like_a/b-sand. 2 hits.
KO	K00198.
Pfam	PF03063. Prismane. 1 hit. [Graphical view]
PIRSF	PIRSF005023. CODH. 1 hit.
SUPFAM	SSF56821. Prismane_like. 1 hit.
TIGRFAMs	TIGR01702. CO_DH_cata. 1 hit.
ProtoNet	Search...

Entry information

Entry name

COOS_METKA

Accession

Primary (citable) accession number: Q8TXX3
Secondary accession number(s): Q9P9A2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	June 1, 2002
Last modified:	November 16, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of page

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents