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

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Reviewed, UniProtKB/Swiss-Prot P27988 (DCMA_MOOTH)

Last modified June 16, 2009. Version 64. 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 alpha Short name=CODH/ACS Short name=Acetyl-CoA synthase subunit Short name=ACS subunit EC=2.3.1.169
Organism	Moorella thermoacetica (Clostridium thermoaceticum)
Taxonomic identifier	1525 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Moorella group › Moorella

Protein attributes

Sequence length	729 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The beta subunit generates CO from CO₂, while the alpha subunit (this protein) 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	Acetyl-CoA + corrinoid protein = CO + methylcorrinoid protein + CoA.
Cofactor	Binds 2 nickel ions per subunit. Binds 1 4Fe-4S cluster per subunit.
Subunit structure	Tetramer of two alpha and two beta chains.

Ontologies

Keywords
Biological process	Carbon dioxide fixation
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Nickel
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	acetyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro carbon utilization by fixation of carbon dioxide Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW CO-methylating acetyl-CoA synthase activity Inferred from electronic annotation. Source: EC carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: InterPro 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

729

Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha

PRO_0000079807

Sites

Metal binding

1

Iron-sulfur (4Fe-4S)

Metal binding

1

Iron-sulfur (4Fe-4S)

Metal binding

1

Nickel 1

Metal binding

1

Iron-sulfur (4Fe-4S)

Metal binding

1

Iron-sulfur (4Fe-4S)

Metal binding

1

Nickel 1

Metal binding

1

Nickel 2

Metal binding

1

Nickel 1; via amide nitrogen

Metal binding

1

Nickel 2; via amide nitrogen

Metal binding

1

Nickel 1

Metal binding

1

Nickel 2

Secondary structure

1

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729

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P27988-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 619BB19D959F5A72
Show »

729

81,725

        10         20         30         40         50         60 
MTDFDKIFEG AIPEGKEPVA LFREVYHGAI TATSYAEILL NQAIRTYGPD HPVGYPDTAY 

        70         80         90        100        110        120 
YLPVIRCFSG EEVKKLGDLP PILNRKRAQV SPVLNFENAR LAGEATWYAA EIIEALRYLK 

       130        140        150        160        170        180 
YKPDEPLLPP PWTGFIGDPV VRRFGIKMVD WTIPGEAIIL GRAKDSKALA KIVKELMGMG 

       190        200        210        220        230        240 
FMLFICDEAV EQLLEENVKL GIDYIAYPLG NFTQIVHAAN YALRAGMMFG GVTPGAREEQ 

       250        260        270        280        290        300 
RDYQRRRIRA FVLYLGEHDM VKTAAAFGAI FTGFPVITDQ PLPEDKQIPD WFFSVEDYDK 

       310        320        330        340        350        360 
IVQIAMETRG IKLTKIKLDL PINFGPAFEG ESIRKGDMYV EMGGNRTPAF ELVRTVSESE 

       370        380        390        400        410        420 
ITDGKIEVIG PDIDQIPEGS KLPLGILVDI YGRKMQADFE GVLERRIHDF INYGEGLWHT 

       430        440        450        460        470        480 
GQRNINWLRV SKDAVAKGFR FKNYGEILVA KMKEEFPAIV DRVQVTIFTD EAKVKEYMEV 

       490        500        510        520        530        540 
AREKYKERDD RMRGLTDETV DTFYSCVLCQ SFAPNHVCIV TPERVGLCGA VSWLDAKASY 

       550        560        570        580        590        600 
EINHAGPNQP IPKEGEIDPI KGIWKSVNDY LYTASNRNLE QVCLYTLMEN PMTSCGCFEA 

       610        620        630        640        650        660 
IMAILPECNG IMITTRDHAG MTPSGMTFST LAGMIGGGTQ TPGFMGIGRT YIVSKKFISA 

       670        680        690        700        710        720 
DGGIARIVWM PKSLKDFLHD EFVRRSVEEG LGEDFIDKIA DETIGTTVDE ILPYLEEKGH 


PALTMDPIM

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]	"Identification of a cysteine involved in the interaction between carbon monoxide dehydrogenase and corrinoid/Fe-S protein from Clostridium thermoaceticum." Shanmugasundaram T., Sundaresh C.S., Kumar G.K. FEBS Lett. 326:281-284(1993) [PubMed: 8325380] [Abstract] Cited for: PROTEIN SEQUENCE OF 494-508.
[3]	"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).
[4]	"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

M62727 Genomic DNA. Translation: AAA23229.1.

PIR

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MJG	X-ray	2.20	M/N/O/P	1-729	[»]
1OAO	X-ray	1.90	C/D	1-729	[»]
2Z8Y	X-ray	2.51	M/N/O/P	1-729	[»]

ModBase

Enzyme and pathway databases

BRENDA

2.3.1.169. 14822.

Family and domain databases

InterPro

IPR004461. CO_DH/Ac-CoA_synth_bsu.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]

Gene3D

G3DSA:3.40.50.2030. Prismane-like_a/b-sand. 1 hit.

Pfam

PF03598. CdhC. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00316. cdhC. 1 hit.

ProtoNet

Entry information

Entry name

DCMA_MOOTH

Accession

Primary (citable) accession number: P27988

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 64 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