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O27745 (ACDB_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA decarbonylase/synthase complex subunit beta

Short name=ACDS complex subunit beta
EC=2.3.1.-
Alternative name(s):
ACDS complex acyltransferase
Gene names
Name:cdhC
Ordered Locus Names:MTH_1710
OrganismMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO2 By similarity. HAMAP-Rule MF_01138

Catalytic activity

Acetyl-CoA + [acetyl-CoA decarbonylase/synthase complex beta subunit] = CoA + acetyl-[acetyl-CoA decarbonylase/synthase complex beta subunit]. HAMAP-Rule MF_01138

Cofactor

Binds 1 nickel-iron-sulfur cluster By similarity. HAMAP-Rule MF_01138

Subunit structure

Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha2epsilon2)(4)-beta(8)-(gamma1delta1)8 Potential.

Sequence similarities

Belongs to the CdhC family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460Acetyl-CoA decarbonylase/synthase complex subunit beta HAMAP-Rule MF_01138
PRO_0000155108

Regions

Compositional bias402 – 41312Glu-rich HAMAP-Rule MF_01138

Sites

Metal binding1881Nickel-iron-sulfur Potential
Metal binding1911Nickel-iron-sulfur Potential
Metal binding2771Nickel-iron-sulfur Potential
Metal binding2791Nickel-iron-sulfur Potential

Sequences

Sequence LengthMass (Da)Tools
O27745 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DB4D50693D154BDA

FASTA46051,737
        10         20         30         40         50         60 
MFEDIPVDVS PMHEGERIRS ANMFVELAGP KSIGAELVQV KDEVEDGKVE VKGPEIDEME 

        70         80         90        100        110        120 
QGQVYPFAIN VEVAGSELEE ELESVIERRL HELCNYVKGF MHLNQRDQIW CRVSTEAKDA 

       130        140        150        160        170        180 
GFRLEHLGKA LSVLFREEFP IIESIAVTLM TDEAAVQEFL ETAREKYETR DSRARELSDE 

       190        200        210        220        230        240 
DVDVFYGCLM CQSFAPTHVC IVTPDRTALC GAINWFDCRA AYKMDPDGPI FEIEKGEVLD 

       250        260        270        280        290        300 
PERGEYANVN AAVEENSQGT TDRVYLHSVF GYPHTSCGCF EAVAFYIPEL DGIGIVNRDF 

       310        320        330        340        350        360 
RGETPLGIPF SAMAGQCSGG KQVEGFSGLS LEYMRSPKFL QADGGYHRVI WMPRELKESV 

       370        380        390        400        410        420 
LEFIPEDVRD KIATEEDATS IKDLRRFLRD NEHPVLERAA VEETEPEEEE VEEAYPEETP 

       430        440        450        460 
IPEGVPVMAA PEMTLPAAGG FRIVLKNAKI YAEKVIIKRK 

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB86182.1.
PIRH69095.
RefSeqNP_276822.1. NC_000916.1.

3D structure databases

ProteinModelPortalO27745.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO27745. 1 interaction.
STRING187420.MTH1710.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB86182; AAB86182; MTH_1710.
GeneID1470795.
KEGGmth:MTH1710.

Phylogenomic databases

eggNOGCOG1614.
KOK00193.
OMAIWCRVSK.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-1713-MONOMER.

Family and domain databases

HAMAPMF_01138. CdhC.
InterProIPR004461. CO_DH/Ac-CoA_synth_bsu.
IPR023432. CO_DH/Ac-CoA_synth_bsu_arc.
IPR011254. Prismane-like.
[Graphical view]
PfamPF03598. CdhC. 1 hit.
[Graphical view]
SUPFAMSSF56821. SSF56821. 1 hit.
TIGRFAMsTIGR00316. cdhC. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACDB_METTH
AccessionPrimary (citable) accession number: O27745
Entry history
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families