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Q49161

- ACDA1_METMA

UniProt

Q49161 - ACDA1_METMA

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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: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

CO + H2O + A = CO2 + AH2.

Cofactori

Binds 7 4Fe-4S clusters per heterotetramer.Curated
Binds 2 nickel-iron-sulfur clusters per heterotetramer.Curated

pH dependencei

Optimum pH is 8-9.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S); shared with dimeric partnerBy similarity
Metal bindingi76 – 761Iron-sulfur 1 (4Fe-4S); shared with dimeric partnerBy similarity
Metal bindingi77 – 771Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi79 – 791Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi84 – 841Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi94 – 941Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi250 – 2501Nickel-iron-sulfurBy similarity
Metal bindingi278 – 2781Nickel-iron-sulfurBy similarity
Metal bindingi323 – 3231Nickel-iron-sulfurBy similarity
Metal bindingi417 – 4171Iron-sulfur 3 (4Fe-4S)Sequence Analysis
Metal bindingi420 – 4201Iron-sulfur 3 (4Fe-4S)Sequence Analysis
Metal bindingi423 – 4231Iron-sulfur 3 (4Fe-4S)Sequence Analysis
Metal bindingi427 – 4271Iron-sulfur 3 (4Fe-4S)Sequence Analysis
Metal bindingi455 – 4551Iron-sulfur 4 (4Fe-4S)Sequence Analysis
Metal bindingi458 – 4581Iron-sulfur 4 (4Fe-4S)Sequence Analysis
Metal bindingi461 – 4611Iron-sulfur 4 (4Fe-4S)Sequence Analysis
Metal bindingi465 – 4651Iron-sulfur 4 (4Fe-4S)Sequence Analysis
Metal bindingi523 – 5231Nickel-iron-sulfurBy similarity
Metal bindingi552 – 5521Nickel-iron-sulfurBy similarity
Metal bindingi587 – 5871Nickel-iron-sulfurBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. acetyl-CoA metabolic process Source: InterPro
  2. methanogenesis, from acetate Source: UniProtKB-HAMAP
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 1 (EC:1.2.99.2)
Short name:
ACDS complex subunit alpha 1
Alternative name(s):
ACDS complex carbon monoxide dehydrogenase 1
Short name:
ACDS CODH 1
Gene namesi
Name:cdhA1
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
ProteomesiUP000000595: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 806805Acetyl-CoA decarbonylase/synthase complex subunit alpha 1PRO_0000155080Add
BLAST

Interactioni

Subunit structurei

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).Curated

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 1Add
BLAST
Domaini445 – 475314Fe-4S ferredoxin-type 2Add
BLAST

Domaini

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.

Sequence similaritiesi

Contains 2 4Fe-4S ferredoxin-type domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1152.
HOGENOMiHOG000224351.
KOiK00192.
OMAiRNEREIP.

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]
PfamiPF13183. Fer4_8. 1 hit.
PF03063. 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:
EMBL
GenBank
DDBJ
Links Updated
L26487 Genomic DNA. Translation: AAC37044.1.
AE008384 Genomic DNA. Translation: AAM31785.1.
RefSeqiNP_634113.1. NC_003901.1.
WP_011034020.1. NC_003901.1.

Genome annotation databases

EnsemblBacteriaiAAM31785; AAM31785; MM_2089.
GeneIDi1480431.
KEGGimma:MM_2089.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L26487 Genomic DNA. Translation: AAC37044.1 .
AE008384 Genomic DNA. Translation: AAM31785.1 .
RefSeqi NP_634113.1. NC_003901.1.
WP_011034020.1. NC_003901.1.

3D structure databases

ProteinModelPortali Q49161.
SMRi Q49161. Positions 43-804.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 192952.MM_2089.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM31785 ; AAM31785 ; MM_2089 .
GeneIDi 1480431.
KEGGi mma:MM_2089.

Phylogenomic databases

eggNOGi COG1152.
HOGENOMi HOG000224351.
KOi K00192.
OMAi RNEREIP.

Enzyme and pathway databases

UniPathwayi UPA00642 .
BioCyci MMAZ192952:GCK2-2143-MONOMER.

Family and domain databases

Gene3Di 3.40.50.2030. 2 hits.
HAMAPi MF_01137. CdhA.
InterProi IPR017896. 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 ]
Pfami PF13183. Fer4_8. 1 hit.
PF03063. Prismane. 2 hits.
[Graphical view ]
SUPFAMi SSF46548. SSF46548. 1 hit.
SSF56821. SSF56821. 1 hit.
TIGRFAMsi TIGR00314. cdhA. 1 hit.
PROSITEi PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: October 1, 2014
This is version 104 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

External Data

Dasty 3