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Protein

Acetyl-CoA decarbonylase/synthase complex subunit alpha 1

Gene

cdhA1

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.UniRule annotation

Catalytic activityi

CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterUniRule annotationNote: Binds 7 [4Fe-4S] clusters per heterotetramer.UniRule annotation
  • [Ni-4Fe-4S] clusterUniRule annotationNote: Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.UniRule annotation

pH dependencei

Optimum pH is 8-9.

Pathwayi: methanogenesis from acetate

This protein is involved in the pathway methanogenesis from acetate, which is part of One-carbon metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway methanogenesis from acetate and in One-carbon metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S); shared with dimeric partnerUniRule annotation
Metal bindingi76 – 761Iron-sulfur 2 (4Fe-4S)UniRule annotation
Metal bindingi77 – 771Iron-sulfur 1 (4Fe-4S); shared with dimeric partnerUniRule annotation
Metal bindingi79 – 791Iron-sulfur 2 (4Fe-4S)UniRule annotation
Metal bindingi84 – 841Iron-sulfur 2 (4Fe-4S)UniRule annotation
Metal bindingi94 – 941Iron-sulfur 2 (4Fe-4S)UniRule annotation
Binding sitei117 – 1171Carbon monoxide; via tele nitrogenUniRule annotation
Metal bindingi250 – 2501Nickel-iron-sulfur (Ni-4Fe-4S); via tele nitrogenUniRule annotation
Metal bindingi278 – 2781Nickel-iron-sulfur (Ni-4Fe-4S)UniRule annotation
Metal bindingi323 – 3231Nickel-iron-sulfur (Ni-4Fe-4S)UniRule annotation
Metal bindingi417 – 4171Iron-sulfur 3 (4Fe-4S)UniRule annotation
Metal bindingi420 – 4201Iron-sulfur 3 (4Fe-4S)UniRule annotation
Metal bindingi423 – 4231Iron-sulfur 3 (4Fe-4S)UniRule annotation
Metal bindingi427 – 4271Iron-sulfur 4 (4Fe-4S)UniRule annotation
Metal bindingi455 – 4551Iron-sulfur 4 (4Fe-4S)UniRule annotation
Metal bindingi458 – 4581Iron-sulfur 4 (4Fe-4S)UniRule annotation
Metal bindingi461 – 4611Iron-sulfur 4 (4Fe-4S)UniRule annotation
Metal bindingi465 – 4651Iron-sulfur 3 (4Fe-4S)UniRule annotation
Metal bindingi523 – 5231Nickel-iron-sulfur (Ni-4Fe-4S)UniRule annotation
Metal bindingi552 – 5521Nickel-iron-sulfur (Ni-4Fe-4S)UniRule annotation
Metal bindingi587 – 5871Nickel-iron-sulfur (Ni-4Fe-4S)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanogenesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, Nickel

Enzyme and pathway databases

BioCyciMMAZ192952:GCK2-2143-MONOMER.
UniPathwayiUPA00642.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA decarbonylase/synthase complex subunit alpha 1UniRule annotation (EC:1.2.7.4UniRule annotation)
Short name:
ACDS complex subunit alpha 1UniRule annotation
Alternative name(s):
ACDS complex carbon monoxide dehydrogenase subunit alpha 1UniRule annotation
Short name:
ACDS CODH subunit alpha 1UniRule annotation
Gene namesi
Name:cdhA1UniRule annotation
Ordered Locus Names:MM_2089
OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Taxonomic identifieri192952 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
Proteomesi
  • UP000000595 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 806805Acetyl-CoA decarbonylase/synthase complex subunit alpha 1PRO_0000155080Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha2epsilon2)(4)-beta(8)-(gamma1delta1)8.UniRule annotation

Protein-protein interaction databases

STRINGi192952.MM_2089.

Structurei

3D structure databases

ProteinModelPortaliQ49161.
SMRiQ49161. Positions 43-804.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini406 – 436314Fe-4S ferredoxin-type 1UniRule annotationAdd
BLAST
Domaini445 – 475314Fe-4S ferredoxin-type 2UniRule annotationAdd
BLAST

Domaini

Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.UniRule annotation

Sequence similaritiesi

Belongs to the Ni-containing carbon monoxide dehydrogenase family.UniRule annotation
Contains 2 4Fe-4S ferredoxin-type domains.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiarCOG02428. Archaea.
COG1152. LUCA.
HOGENOMiHOG000224351.
KOiK00192.
OMAiVANSHIA.

Family and domain databases

Gene3Di3.40.50.2030. 2 hits.
HAMAPiMF_01137. CdhA.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR004460. CO_DH/Ac-CoA_synth_asu.
IPR004137. HCP/CODH.
IPR009051. Helical_ferredxn.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]
PfamiPF03063. Prismane. 2 hits.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR00314. cdhA. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q49161-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLTTGSFS IEDLESVQIT INNIVGAAKE AAEEKTKELG HMGPTPFPGL
60 70 80 90 100
ETYRDDWNLK LLDRYEPVVT PMCDQCCYCT YGPCDLSNNK RGACGIDMLG
110 120 130 140 150
HNGREFFLRV ITGTACHAAH GRHLLDHLIE VFGEELPLNL GQSDVLTPNI
160 170 180 190 200
TITTGQRPQT LGEIKPAMEH VEEQLTQLLA TVHAGQESAE IDYDSKALFS
210 220 230 240 250
GSLDHVGMEI SDIVQIAALD FPKADPEAPL IEMGMGTIDK DKPFLCVIGH
260 270 280 290 300
NVGGVTYMMD YMEEHELTDK VELGGLCCTA IDLTRYKEAD RRPPYTKVVG
310 320 330 340 350
SMSKELKIIR SGMPDVIVVD EQCVRGDIVP EAQKLKIPVI ASNAKIMYGL
360 370 380 390 400
PNRTDAGVEE TIEELKSGAI PGAVILDYEK LGEISVRLAQ EMHPIREAAG
410 420 430 440 450
VREIPSDEQL KEWVDKCADC GACYLACPIE LDIPEAMKFA KQGDFSYLED
460 470 480 490 500
LHDACIGCRR CEQVCKKEIP ILSVIEKASQ KIIAEEKGWM RAGRGQVSDA
510 520 530 540 550
EIRAEGLNLV MGTTPGIIAI IGCPNYSDCA KAVYYIAEEF LKRNYIVVGT
560 570 580 590 600
GCGSMDMGMY KDEDGKTLYE RFPGGFQSGG LVNIGSCVSN AHITGAAQKV
610 620 630 640 650
AGIFGGRTME GNLAEIADYV LNRVGACGLA WGAFSQKASS IGTGCNIYGI
660 670 680 690 700
PAVLGAHSSK YRRALIAKNY DESKWKVYDA RNGEEMPIPP APEFLLTTAE
710 720 730 740 750
TWQEAIPMMA KACLRPSDNS LGRSIKLTHW MELHDKYIGG LPEDWWKFIR
760 770 780 790 800
TEADLPLAKR ADLMKKLEAE RGWEIDWKKK KIISGPKIKF DVSAQPTNLK

RLCKGA
Length:806
Mass (Da):88,583
Last modified:January 23, 2007 - v3
Checksum:i8A6EE054FBE778AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26487 Genomic DNA. Translation: AAC37044.1.
AE008384 Genomic DNA. Translation: AAM31785.1.
RefSeqiWP_011034020.1. NC_003901.1.

Genome annotation databases

EnsemblBacteriaiAAM31785; AAM31785; MM_2089.
GeneIDi24840339.
KEGGimma:MM_2089.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26487 Genomic DNA. Translation: AAC37044.1.
AE008384 Genomic DNA. Translation: AAM31785.1.
RefSeqiWP_011034020.1. NC_003901.1.

3D structure databases

ProteinModelPortaliQ49161.
SMRiQ49161. Positions 43-804.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi192952.MM_2089.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM31785; AAM31785; MM_2089.
GeneIDi24840339.
KEGGimma:MM_2089.

Phylogenomic databases

eggNOGiarCOG02428. Archaea.
COG1152. LUCA.
HOGENOMiHOG000224351.
KOiK00192.
OMAiVANSHIA.

Enzyme and pathway databases

UniPathwayiUPA00642.
BioCyciMMAZ192952:GCK2-2143-MONOMER.

Family and domain databases

Gene3Di3.40.50.2030. 2 hits.
HAMAPiMF_01137. CdhA.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR004460. CO_DH/Ac-CoA_synth_asu.
IPR004137. HCP/CODH.
IPR009051. Helical_ferredxn.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]
PfamiPF03063. Prismane. 2 hits.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR00314. cdhA. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Carbon monoxide dehydrogenase from Methanosarcina frisia Go1. Characterization of the enzyme and the regulated expression of two operon-like cdh gene clusters."
    Eggen R.I.L., van Kranenburg R., Vriesema A.J.M., Geerling A.C.M., Verhagen M.F.J.M., Hagen W.R., de Vos W.M.
    J. Biol. Chem. 271:14256-14263(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-12.
    Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.
  2. "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
    Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R.
    , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
    J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Entry informationi

Entry nameiACDA1_METMA
AccessioniPrimary (citable) accession number: Q49161
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.