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UniProtKB/Swiss-Prot entry P27988


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DCMA_MOOTH
Primary accession number P27988
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 62)
Name and origin of the protein
Protein name Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha
Synonyms CODH/ACS
Acetyl-CoA synthase subunit
ACS subunit
EC 2.3.1.169
Gene name None
From
Moorella thermoacetica (Clostridium thermoaceticum) [TaxID: 1525] 
Taxonomy Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; Thermoanaerobacteraceae; Moorella group; Moorella.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1748656 [NCBI, ExPASy, EBI, Israel, Japan]
Morton T.A., Runquist J.A., Ragsdale S.W., Shanmugasundaram T., Wood H.G., Ljungdahl L.G.;
"The primary structure of the subunits of carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum.";
J. Biol. Chem. 266:23824-23828(1991).
[2]
PROTEIN SEQUENCE OF 494-508.
DOI=10.1016/0014-5793(93)81808-D; PubMed=8325380 [NCBI, ExPASy, EBI, Israel, Japan]
Shanmugasundaram T., Sundaresh C.S., Kumar G.K.;
"Identification of a cysteine involved in the interaction between carbon monoxide dehydrogenase and corrinoid/Fe-S protein from Clostridium thermoaceticum.";
FEBS Lett. 326:281-284(1993).
[3]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1126/science.1075843; PubMed=12386327 [NCBI, ExPASy, EBI, Israel, Japan]
Doukov T.I., Iverson T.M., Seravalli J., Ragsdale S.W., Drennan C.L.;
"A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase.";
Science 298:567-572(2002).
[4]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1038/nsb912; PubMed=12627225 [NCBI, ExPASy, EBI, Israel, Japan]
Darnault C., Volbeda A., Kim E.J., Legrand P., Vernede X., Lindahl P.A., Fontecilla-Camps J.-C.;
"Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase.";
Nat. Struct. Biol. 10:271-279(2003).
Comments
  • FUNCTION: The beta subunit generates CO from CO(2), 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.
  • COFACTOR: Binds 1 4Fe-4S cluster per subunit.
  • SUBUNIT: Tetramer of two alpha and two beta chains.
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
M62727; AAA23229.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B41670; B41670.
3D structure databases
PDB
1MJG; X-ray; 2.20 A; M/N/O/P=1-729.[ExPASy / RCSB / EBI]
1OAO; X-ray; 1.90 A; C/D=1-729.[ExPASy / RCSB / EBI]
2Z8Y; X-ray; 2.51 A; M/N/O/P=1-729.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1MJG; -.
1OAO; -.
2Z8Y; -.
ModBase P27988.
Ontologies
GO
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0018492; Molecular function: carbon-monoxide dehydrogenase (acceptor) activity (inferred from electronic annotation from InterPro).
GO:0043884; Molecular function: CO-methylating acetyl-CoA synthase activity (inferred from electronic annotation from EC).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016151; Molecular function: nickel ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006084; Biological process: acetyl-CoA metabolic process (inferred from electronic annotation from InterPro).
GO:0015977; Biological process: carbon utilization by fixation of carbon dioxide (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004461; CO_DHase/Ac-CoA_synth_bsu.
IPR016099; Prismane-like_a/b-sand.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.2030; Prismane-like_a/b-sand; 1.
Pfam PF03598; CdhC; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00316; cdhC; 1.
ProtoNet P27988.
Other
LinkHub P27988; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 4Fe-4S; Carbon dioxide fixation; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; Nickel; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   729  729     Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha. PRO_0000079807
METAL   506   506        Iron-sulfur (4Fe-4S). 
METAL   509   509        Iron-sulfur (4Fe-4S). 
METAL   509   509        Nickel 1. 
METAL   518   518        Iron-sulfur (4Fe-4S). 
METAL   528   528        Iron-sulfur (4Fe-4S). 
METAL   595   595        Nickel 1. 
METAL   595   595        Nickel 2. 
METAL   596   596        Nickel 1; via amide nitrogen. 
METAL   596   596        Nickel 2; via amide nitrogen. 
METAL   597   597        Nickel 1. 
METAL   597   597        Nickel 2. 
HELIX   4     8  5      
HELIX   19    47  29      
STRAND   59    62  4      
HELIX   63    68  6      
HELIX   76    78  3      
HELIX   79    88  10      
HELIX   96   117  22      
HELIX   118   120  3      
HELIX   138   143  6      
HELIX   145   148  4      
TURN   149   151  3      
STRAND   156   161  6      
HELIX   166   178  13      
STRAND   182   186  5      
HELIX   189   195  7      
HELIX   202   204  3      
STRAND   206   211  6      
HELIX   212   215  4      
HELIX   216   228  13      
HELIX   237   247  11      
STRAND   250   257  8      
HELIX   260   271  12      
STRAND   276   280  5      
HELIX   284   286  3      
TURN   289   291  3      
STRAND   292   294  3      
TURN   298   300  3      
HELIX   301   309  9      
HELIX   326   328  3      
HELIX   335   337  3      
STRAND   338   343  6      
STRAND   349   355  7      
HELIX   358   360  3      
STRAND   366   370  5      
HELIX   373   375  3      
STRAND   384   391  8      
HELIX   397   412  16      
STRAND   417   419  3      
STRAND   427   431  5      
HELIX   432   437  6      
HELIX   442   455  14      
STRAND   460   468  9      
HELIX   471   493  23      
TURN   497   499  3      
STRAND   501   506  6      
HELIX   508   511  4      
STRAND   518   521  4      
HELIX   533   542  10      
STRAND   550   552  3      
STRAND   555   558  4      
TURN   559   562  4      
HELIX   565   574  10      
STRAND   587   590  4      
STRAND   599   605  7      
HELIX   606   608  3      
STRAND   610   615  6      
HELIX   628   635  8      
STRAND   644   647  4      
HELIX   649   653  5      
TURN   655   658  4      
HELIX   659   661  3      
HELIX   663   666  4      
STRAND   667   669  3      
HELIX   672   688  17      
HELIX   695   698  4      
TURN   702   704  3      
HELIX   708   717  10      
HELIX   721   724  4      
Sequence information
Length: 729 AA [This is the length of the unprocessed precursor] Molecular weight: 81725 Da [This is the MW of the unprocessed precursor] CRC64: 619BB19D959F5A72 [This is a checksum on the sequence]
        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 

P27988 in FASTA format

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