Reviewed, UniProtKB/Swiss-Prot P26692 (ACDA_METSO)

Names and origin

Protein names

Recommended name:
    Acetyl-CoA decarbonylase/synthase complex subunit alpha
      Short name=ACDS complex subunit alpha
    EC=1.2.99.2
Alternative name(s):
    ACDS complex carbon monoxide dehydrogenase
      Short name=ACDS CODH

Gene names

Name:

cdhA

Organism

Methanothrix soehngenii

Taxonomic identifier

2223 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosaetaceae › Methanosaeta

Protein attributes

Sequence length	793 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO2 By similarity. HAMAP MF_01137
Catalytic activity	CO + H2O + A = CO2 + AH2. HAMAP MF_01137
Cofactor	Binds 7 4Fe-4S clusters per heterotetramer Potential. HAMAP MF_01137 Binds 2 nickel-iron-sulfur clusters per heterotetramer Potential. HAMAP MF_01137
Subunit structure	Heterotetramer of two alpha and two epsilon chains. 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. HAMAP MF_01137
Domain	Cluster B is an all-cysteinyl-liganded 4Fe4S cluster; cluster C is a mixed Ni-Fe-S cluster which appears to be the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe4S cluster that bridges the two subunits of the CODH dimer. May contain two additional 4Fe-4S clusters, dubbed E and F, that might reroute electron transfer along different paths. HAMAP MF_01137
Sequence similarities	Belongs to the Ni-containing carbon monoxide dehydrogenase family. Contains 2 4Fe-4S ferredoxin-type domains.
Caution	This protein lacks the conserved Cys in positions 52 and 56; they are replaced by an Asp and a Thr, respectively. It is therefore possible that the C- and D-clusters are either altered or missing in this protein, which may not form heterotetramers.

Ontologies

Keywords
Domain	Repeat
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Nickel
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	acetyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro generation of precursor metabolites and energy Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: HAMAP electron carrier 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	1 – 793	793	Acetyl-CoA decarbonylase/synthase complex subunit alpha HAMAP MF_01137		PRO_0000155082
Regions
	Domain	393 – 422	30	4Fe-4S ferredoxin-type 1
	Domain	432 – 461	30	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	55	1	Iron-sulfur 1 (4Fe-4S); shared with dimeric partner By similarity
	Metal binding	58	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	63	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	73	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	229	1	Nickel-iron-sulfur By similarity
	Metal binding	257	1	Nickel-iron-sulfur By similarity
	Metal binding	309	1	Nickel-iron-sulfur By similarity
	Metal binding	403	1	Iron-sulfur 3 (4Fe-4S) Potential
	Metal binding	406	1	Iron-sulfur 3 (4Fe-4S) Potential
	Metal binding	409	1	Iron-sulfur 3 (4Fe-4S) Potential
	Metal binding	413	1	Iron-sulfur 3 (4Fe-4S) Potential
	Metal binding	441	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	444	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	447	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	451	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	509	1	Nickel-iron-sulfur By similarity
	Metal binding	538	1	Nickel-iron-sulfur By similarity
	Metal binding	573	1	Nickel-iron-sulfur By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26692-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 7CBCB187B1860A2B	FASTA	793	88,152
	10 20 30 40 50 60 MKNVQINIGA VVKEEDEWDQ EMGPFPKPGV ATLRDWDFKI CNRYKIMYSP ADDTCTLCTY 70 80 90 100 110 120 GPCDLTGNKK GACGIDMAAA CGKIVLVAVL MGTCAHTAHG RHLYHWCLDK FGDMPFDMGS 130 140 150 160 170 180 EILVDAPLYR TILGKKPKSL KDFGEALEYC EEEIVQLLAA CHTGQEGHYM DFESKSLHSG 190 200 210 220 230 240 MIDSLGKEIC DMLQTVAYDM PRGAADAPLV EIGMGTLDQN KGVLIAYGHN LAAGAEAMIY 250 260 270 280 290 300 TEEHNLWDKV DIGGVCCTAI DLTRITETGR ESKIPANLGP KAKVAGAMGW WRKMVRAGIM 310 320 330 340 350 360 DTVIVDEQCV FCDVLEDCQQ RHIPVIASND KIMLGLPDRT NDSADAIVED LVSFKMPGVA 370 380 390 400 410 420 ILDPVKAGEV AIRTAVAVKP KREQYKKESL FTEQQFKDTL ATCTECNQCA FVCPPHIRIS 430 440 450 460 470 480 EMISEALKGN LEPFSSTYEV CVGCQRCEQT CPQEIPILKL YEYANREYIR NQKFKMRAGR 490 500 510 520 530 540 GPVLDTEIRK VGAPLVLGQI PGVIALVGCS NYPNGTKECY DIAKEFVDRG YIVVATGCMA 550 560 570 580 590 600 MDMSLYKDED GKTIWEQYEG AFDGRNICNI GSCVANAHIH GAAIKVATIF AHRNERANYD 610 620 630 640 650 660 DIADYIMSKV GACGVAWGAY SQKAASIATG VNRIGIPVVV QPSSVIYRRT FMGRTDKPED 670 680 690 700 710 720 WMVIDAKNGN MQQIEPAPEA MLYIAETKEE AMLEMAKLCF RPSDNTQGRG IKLTHYCDIS 730 740 750 760 770 780 MKYFGKLPDD WHLFVRDVKD LPLNYQTQMM KELEEKHGWK IDWKAKKFIS GPLRPADVSF 790 DPTNIPRKIR AKK

References

[1]

"Cloning, expression, and sequence analysis of the genes for carbon monoxide dehydrogenase of Methanothrix soehngenii." Eggen R.I.L., Geerling A.C.M., Jetten M.S.M., de Vos W.M. J. Biol. Chem. 266:6883-6887(1991) [PubMed: 1901858] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: Opfikon / DSM 2139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M55280 Genomic DNA. Translation: AAA72934.1.
PIR	A39764.
3D structure databases
SMR	P26692. Positions 22-791.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.99.2. 267.
Family and domain databases
HAMAP	MF_01137. CdhA. [Tree]
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR004460. CO_DH/Ac-CoA_synth_asu. IPR016101. CO_DH_a-bundle. IPR009051. Helical_ferredxn. IPR004137. Prismane. IPR011254. Prismane-like. IPR016099. Prismane-like_a/b-sand. [Graphical view]
Gene3D	G3DSA:1.20.1270.30. CO_DH_a-bundle. 1 hit. G3DSA:3.40.50.2030. Prismane-like_a/b-sand. 2 hits.
Pfam	PF03063. Prismane. 2 hits. [Graphical view]
TIGRFAMs	TIGR00314. cdhA. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACDA_METSO

Accession

Primary (citable) accession number: P26692

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	February 9, 2010
This is version 65 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)