O27745 (ACDB_METTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter › Methanobacterium thermoformicicum

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Protein existence	Inferred 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.
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.

Ontologies

Keywords
Ligand	Iron Iron-sulfur Metal-binding Nickel
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	acetyltransferase activity Inferred from electronic annotation. Source: HAMAP carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: HAMAP iron-sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW nickel cation binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 460	460	Acetyl-CoA decarbonylase/synthase complex subunit beta HAMAP-Rule MF_01138		PRO_0000155108
Regions
	Compositional bias	402 – 413	12	Glu-rich HAMAP-Rule MF_01138
Sites
	Metal binding	188	1	Nickel-iron-sulfur Potential
	Metal binding	191	1	Nickel-iron-sulfur Potential
	Metal binding	277	1	Nickel-iron-sulfur Potential
	Metal binding	279	1	Nickel-iron-sulfur Potential

Sequences

	Sequence		Length	Mass (Da)
	O27745 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: DB4D50693D154BDA	FASTA	460	51,737
	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

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. , 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.
PIR	H69095.
RefSeq	NP_276822.1. NC_000916.1.
3D structure databases
ProteinModelPortal	O27745.
ModBase	Search...
Protein-protein interaction databases
IntAct	O27745. 1 interaction.
STRING	187420.MTH1710.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB86182; AAB86182; MTH_1710.
GeneID	1470795.
KEGG	mth:MTH1710.
Phylogenomic databases
eggNOG	COG1614.
KO	K00193.
OMA	TPMGIPF.
ProtClustDB	PRK04456.
Enzyme and pathway databases
BioCyc	MTHE187420:GJNM-1713-MONOMER.
Family and domain databases
HAMAP	MF_01138. CdhC.
InterPro	IPR004461. CO_DH/Ac-CoA_synth_bsu. IPR023432. CO_DH/Ac-CoA_synth_bsu_arc. IPR011254. Prismane-like. [Graphical view]
Pfam	PF03598. CdhC. 1 hit. [Graphical view]
SUPFAM	SSF56821. Prismane_like. 1 hit.
TIGRFAMs	TIGR00316. cdhC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACDB_METTH

Accession

Primary (citable) accession number: O27745

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 21, 2003
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program