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Protein

Acetyl-CoA decarbonylase/synthase complex subunit beta

Gene

cdhC

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO2.UniRule annotation

Catalytic activityi

Acetyl-CoA + [acetyl-CoA decarbonylase/synthase complex beta subunit] = CoA + acetyl-[acetyl-CoA decarbonylase/synthase complex beta subunit].UniRule annotation

Cofactori

[Ni-Fe-S] clusterUniRule annotationNote: Binds 1 [Ni-Fe-S] cluster.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi188 – 1881Nickel-iron-sulfurUniRule annotation
Metal bindingi191 – 1911Nickel-iron-sulfurUniRule annotation
Metal bindingi277 – 2771Nickel-iron-sulfurUniRule annotation
Metal bindingi279 – 2791Nickel-iron-sulfurUniRule annotation

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB-HAMAP
  2. carbon-monoxide dehydrogenase (acceptor) activity Source: InterPro
  3. iron ion binding Source: UniProtKB-HAMAP
  4. iron-sulfur cluster binding Source: UniProtKB-KW
  5. nickel cation binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. acetyl-CoA metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Iron, Iron-sulfur, Metal-binding, Nickel

Enzyme and pathway databases

BioCyciMTHE187420:GJNM-1713-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA decarbonylase/synthase complex subunit betaUniRule annotation (EC:2.3.1.-UniRule annotation)
Short name:
ACDS complex subunit betaUniRule annotation
Alternative name(s):
ACDS complex acyltransferaseUniRule annotation
Gene namesi
Name:cdhCUniRule annotation
Ordered Locus Names:MTH_1710
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000005223 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Acetyl-CoA decarbonylase/synthase complex subunit betaPRO_0000155108Add
BLAST

Interactioni

Subunit structurei

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.UniRule annotation

Protein-protein interaction databases

IntActiO27745. 1 interaction.
STRINGi187420.MTH1710.

Structurei

3D structure databases

ProteinModelPortaliO27745.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi402 – 41312Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the CdhC family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1614.
KOiK00193.
OMAiIWCRVSK.

Family and domain databases

HAMAPiMF_01138. CdhC.
InterProiIPR004461. CO_DH/Ac-CoA_synth_bsu.
IPR023432. CO_DH/Ac-CoA_synth_bsu_arc.
IPR011254. Prismane-like.
[Graphical view]
PfamiPF03598. CdhC. 1 hit.
[Graphical view]
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR00316. cdhC. 1 hit.

Sequencei

Sequence statusi: Complete.

O27745-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEDIPVDVS PMHEGERIRS ANMFVELAGP KSIGAELVQV KDEVEDGKVE
60 70 80 90 100
VKGPEIDEME QGQVYPFAIN VEVAGSELEE ELESVIERRL HELCNYVKGF
110 120 130 140 150
MHLNQRDQIW CRVSTEAKDA GFRLEHLGKA LSVLFREEFP IIESIAVTLM
160 170 180 190 200
TDEAAVQEFL ETAREKYETR DSRARELSDE DVDVFYGCLM CQSFAPTHVC
210 220 230 240 250
IVTPDRTALC GAINWFDCRA AYKMDPDGPI FEIEKGEVLD PERGEYANVN
260 270 280 290 300
AAVEENSQGT TDRVYLHSVF GYPHTSCGCF EAVAFYIPEL DGIGIVNRDF
310 320 330 340 350
RGETPLGIPF SAMAGQCSGG KQVEGFSGLS LEYMRSPKFL QADGGYHRVI
360 370 380 390 400
WMPRELKESV LEFIPEDVRD KIATEEDATS IKDLRRFLRD NEHPVLERAA
410 420 430 440 450
VEETEPEEEE VEEAYPEETP IPEGVPVMAA PEMTLPAAGG FRIVLKNAKI
460
YAEKVIIKRK
Length:460
Mass (Da):51,737
Last modified:December 31, 1997 - v1
Checksum:iDB4D50693D154BDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB86182.1.
PIRiH69095.
RefSeqiNP_276822.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB86182; AAB86182; MTH_1710.
GeneIDi1470795.
KEGGimth:MTH1710.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB86182.1.
PIRiH69095.
RefSeqiNP_276822.1. NC_000916.1.

3D structure databases

ProteinModelPortaliO27745.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO27745. 1 interaction.
STRINGi187420.MTH1710.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB86182; AAB86182; MTH_1710.
GeneIDi1470795.
KEGGimth:MTH1710.

Phylogenomic databases

eggNOGiCOG1614.
KOiK00193.
OMAiIWCRVSK.

Enzyme and pathway databases

BioCyciMTHE187420:GJNM-1713-MONOMER.

Family and domain databases

HAMAPiMF_01138. CdhC.
InterProiIPR004461. CO_DH/Ac-CoA_synth_bsu.
IPR023432. CO_DH/Ac-CoA_synth_bsu_arc.
IPR011254. Prismane-like.
[Graphical view]
PfamiPF03598. CdhC. 1 hit.
[Graphical view]
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR00316. cdhC. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Entry informationi

Entry nameiACDB_METTH
AccessioniPrimary (citable) accession number: O27745
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 20, 2003
Last sequence update: December 31, 1997
Last modified: March 31, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.