Acetyl-CoA decarbonylase/synthase complex subunit alpha 2

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Reviewed, UniProtKB/Swiss-Prot Q9C4Z4 (ACDA2_METTE)

Last modified February 9, 2010. Version 49. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Acetyl-CoA decarbonylase/synthase complex subunit alpha 2
      Short name=ACDS complex subunit alpha 2
    EC=1.2.99.2
Alternative name(s):
    ACDS complex carbon monoxide dehydrogenase 2
      Short name=ACDS CODH 2

Gene names

Name:

cdhA2

Organism

Methanosarcina thermophila

Taxonomic identifier

2210 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

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Protein attributes

Sequence length	803 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy 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
Pathway	One-carbon metabolism; methanogenesis from acetate. 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.

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Ontologies

Keywords
Biological process	Methanogenesis
Domain	Repeat
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Nickel
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	acetyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW 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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 803

803

Acetyl-CoA decarbonylase/synthase complex subunit alpha 2 HAMAP MF_01137

PRO_0000155084

Regions

Domain

405 – 433

4Fe-4S ferredoxin-type 1

Domain

443 – 472

4Fe-4S ferredoxin-type 2

Sites

Metal binding

Iron-sulfur 1 (4Fe-4S); shared with dimeric partner By similarity

Metal binding

Iron-sulfur 1 (4Fe-4S); shared with dimeric partner By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

249

Nickel-iron-sulfur By similarity

Metal binding

277

Nickel-iron-sulfur By similarity

Metal binding

322

Nickel-iron-sulfur By similarity

Metal binding

414

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

417

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

420

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

424

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

452

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

455

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

458

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

462

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

520

Nickel-iron-sulfur By similarity

Metal binding

549

Nickel-iron-sulfur By similarity

Metal binding

584

Nickel-iron-sulfur By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9C4Z4-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 1C9565D8E1EAEC14
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FASTA

803

87,738

        10         20         30         40         50         60 
MAKLTTGSFS IEDLESVQIT INNIVGAAKE AAEKAEEELG PMGPTPFPTA ATVRDWSFTL 

        70         80         90        100        110        120 
FDRYEPVYTP MCDQCCYCTF GPCNLEGNRR GACGLDMKGQ AAREFFLRCI TGCACHSAHG 

       130        140        150        160        170        180 
RHLLDHIISI FGEDMPINMG ASNVIAPNIQ LITGRQPKTL GDLKPIMEYV EEELGQLLAT 

       190        200        210        220        230        240 
VHAGQEGAAI DYDNKAMLAG ILDHVGMEVS DIAQVTALGF PKSDPEAPLV EVGMGTLDAS 

       250        260        270        280        290        300 
KPVIIAIGHN VAGVTYIMDY MEDNNLTDKM EIGGLCCTAF DMTRYKREDR KPPYAKIVGT 

       310        320        330        340        350        360 
ISKELKVVRS GIPDVIVIDE QCVRADLVEE GKKLKIPVIA SNEKVMYGLP DRTNDDVDAI 

       370        380        390        400        410        420 
IEDIKTGKIP GCVMLDYEKL GELVPRLAME MAPLREGISA IPSDEEMASL VAKCVACGEC 

       430        440        450        460        470        480 
ALACPEELDI PDAIQAAKEG DFTALDFLHD LCVGCRRCEQ VCNKEIPILS VIDKAAQKAI 

       490        500        510        520        530        540 
AEEKGLVRAG RGQVSDAEIR AEGLNLVMGT TPGVIAIIGC ANYPAGSKDV YRIAEEFLNR 

       550        560        570        580        590        600 
NYIVAVSGCS AMDIGMYKDA DGKTLYERFP GRFERGNILN TGSCVSNSHI SGTCHKVAAI 

       610        620        630        640        650        660 
FAGRNLSGNL AEIADYTLNR VGAVGLAWGA YSQKAAAIGT GCNMYGIPAV LGPHSGKYRR 

       670        680        690        700        710        720 
ALIAKTYDEN KWKVYDSRNG SELDIPPSPE FLITTAETWQ EACVLLAKNC IRPSDNNMGR 

       730        740        750        760        770        780 
SIKLTHWIEL SEKYLGVLPE DWWKFVRHEA DLPLSRREEL LKKLETEHGW EIDWKKKKII 

       790        800 
SGPKIKFDVS SQPTNLKRLC KEA

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References

[1]	"Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase multienzyme complex in methanogens. Catalytic properties and evidence for a binuclear Ni-Ni site." Gencic S., Grahame D.A. J. Biol. Chem. 278:6101-6110(2003) [PubMed: 12464601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 1825 / TM-1.
[2]	"Structure of the Ni/Fe-S protein subcomponent of the acetyl-CoA decarbonylase/synthase complex from Methanosarcina thermophila at 26-A resolution." Kocsis E., Kessel M., DeMoll E., Grahame D.A. J. Struct. Biol. 128:165-174(1999) [PubMed: 10600570] [Abstract] Cited for: ELECTRON MICROSCOPY OF ALPHA-EPSILON COMPLEX.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AF173830 Genomic DNA. Translation: AAG53710.1.
3D structure databases
SMR	Q9C4Z4. Positions 43-802.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.99.2. 8918.
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. 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. 1 hit. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

ACDA2_METTE

Accession

Primary (citable) accession number: Q9C4Z4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 21, 2003
Last sequence update:	June 1, 2001
Last modified:	February 9, 2010
This is version 49 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)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents