Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta - Moorella thermoacetica

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Reviewed, UniProtKB/Swiss-Prot P27989 (DCMB_MOOTH)

Last modified February 9, 2010. Version 73. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names	Recommended name: Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta Short name=CODH/ACS Short name=Carbon monoxide dehydrogenase subunit Short name=CODH subunit EC=1.2.7.4 EC=1.2.99.2
Organism	Moorella thermoacetica (Clostridium thermoaceticum)
Taxonomic identifier	1525 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Moorella group › Moorella

Protein attributes

Sequence length	674 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The beta subunit (this protein) generates CO from CO₂, while the alpha subunit combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the alpha subunit by a corrinoid iron-sulfur protein.
Catalytic activity	CO + H₂O + 2 oxidized ferredoxin = CO₂ + 2 reduced ferredoxin + 2 H⁺. CO + H₂O + A = CO₂ + AH₂.
Cofactor	Binds 1 nickel-iron-sulfur cluster per subunit. Binds 2 4Fe-4S clusters per homodimer.
Subunit structure	Tetramer of two alpha and two beta chains.

Ontologies

Keywords
Biological process	Carbon dioxide fixation Electron transport Transport
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Nickel
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	carbon utilization by fixation of carbon dioxide Inferred from electronic annotation. Source: UniProtKB-KW electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
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 carbon-monoxide dehydrogenase (ferredoxin) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

674

Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta

PRO_0000079808

Sites

Metal binding

1

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

Metal binding

1

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

Metal binding

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

1

Nickel-iron-sulfur (Ni-4Fe-4S); via tele nitrogen

Metal binding

1

Nickel-iron-sulfur (Ni-4Fe-4S)

Metal binding

1

Nickel-iron-sulfur (Ni-4Fe-4S)

Metal binding

1

Nickel-iron-sulfur (Ni-4Fe-4S)

Metal binding

1

Nickel-iron-sulfur (Ni-4Fe-4S)

Metal binding

1

Nickel-iron-sulfur (Ni-4Fe-4S)

Secondary structure

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674

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P27989-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 54BA3D816C25F9FC
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674

72,924

        10         20         30         40         50         60 
MPRFRDLSHN CRPSEAPRVM EPKNRDRTVD PAVLEMLVKS KDDKVITAFD RFVAQQPQCK 

        70         80         90        100        110        120 
IGYEGICCRF CMAGPCRIKA TDGPGSRGIC GASAWTIVAR NVGLMILTGA AAHCEHGNHI 

       130        140        150        160        170        180 
AHALVEMAEG KAPDYSVKDE AKLKEVCRRV GIEVEGKSVL ELAQEVGEKA LEDFRRLKGE 

       190        200        210        220        230        240 
GEATWLMTTI NEGRKEKFRT HNVVPFGIHA SISELVNQAH MGMDNDPVNL VFSAIRVALA 

       250        260        270        280        290        300 
DYTGEHIATD FSDILFGTPQ PVVSEANMGV LDPDQVNFVL HGHNPLLSEI IVQAAREMEG 

       310        320        330        340        350        360 
EAKAAGAKGI NLVGICCTGN EVLMRQGIPL VTSFASQELA ICTGAIDAMC VDVQCIMPSI 

       370        380        390        400        410        420 
SAVAECYHTR IITTADNAKI PGAYHIDYQT ATAIESAKTA IRMAIEAFKE RKESNRPVYI 

       430        440        450        460        470        480 
PQIKNRVVAG WSLEALTKLL ATQNAQNPIR VLNQAILDGE LAGVALICGC NNLKGFQDNS 

       490        500        510        520        530        540 
HLTVMKELLK NNVFVVATGC SAQAAGKLGL LDPANVETYC GDGLKGFLKR LGEGANIEIG 

       550        560        570        580        590        600 
LPPVFHMGSC VDNSRAVDLL MAMANDLGVD TPKVPFVASA PEAMSGKAAA IGTWWVSLGV 

       610        620        630        640        650        660 
PTHVGTMPPV EGSDLIYSIL TQIASDVYGG YFIFEMDPQV AARKILDALE YRTWKLGVHK 

       670 
EVAERYETKL CQGY

References

[1]	"The primary structure of the subunits of carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum." Morton T.A., Runquist J.A., Ragsdale S.W., Shanmugasundaram T., Wood H.G., Ljungdahl L.G. J. Biol. Chem. 266:23824-23828(1991) [PubMed: 1748656] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase." Doukov T.I., Iverson T.M., Seravalli J., Ragsdale S.W., Drennan C.L. Science 298:567-572(2002) [PubMed: 12386327] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[3]	"Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase." Darnault C., Volbeda A., Kim E.J., Legrand P., Vernede X., Lindahl P.A., Fontecilla-Camps J.-C. Nat. Struct. Biol. 10:271-279(2003) [PubMed: 12627225] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M62727 Genomic DNA. Translation: AAA23228.1.

PIR

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MJG	X-ray	2.20	A/B/C/D	1-674	[»]
1OAO	X-ray	1.90	A/B	1-674	[»]
2Z8Y	X-ray	2.51	A/B/C/D	1-674	[»]
3I01	X-ray	2.15	A/B/C/D	1-674	[»]
3I04	X-ray	2.15	A/B/C/D	2-674	[»]

ModBase

Enzyme and pathway databases

BRENDA

1.2.7.4. 14822.
1.2.99.2. 14822.

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.

Pfam

PF03063. Prismane. 1 hit.
[Graphical view]

PIRSF

PIRSF005023. CODH. 1 hit.

TIGRFAMs

TIGR01702. CO_DH_cata. 1 hit.

ProtoNet

Entry information

Entry name

DCMB_MOOTH

Accession

Primary (citable) accession number: P27989

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	February 9, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents