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Q49161

- ACDA1_METMA

UniProt

Q49161 - ACDA1_METMA

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
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

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    MSKLTTGSFS IEDLESVQIT INNIVGAAKE AAEEKTKELG HMGPTPFPGL    50
    ETYRDDWNLK LLDRYEPVVT PMCDQCCYCT YGPCDLSNNK RGACGIDMLG 100
    HNGREFFLRV ITGTACHAAH GRHLLDHLIE VFGEELPLNL GQSDVLTPNI 150
    TITTGQRPQT LGEIKPAMEH VEEQLTQLLA TVHAGQESAE IDYDSKALFS 200
    GSLDHVGMEI SDIVQIAALD FPKADPEAPL IEMGMGTIDK DKPFLCVIGH 250
    NVGGVTYMMD YMEEHELTDK VELGGLCCTA IDLTRYKEAD RRPPYTKVVG 300
    SMSKELKIIR SGMPDVIVVD EQCVRGDIVP EAQKLKIPVI ASNAKIMYGL 350
    PNRTDAGVEE TIEELKSGAI PGAVILDYEK LGEISVRLAQ EMHPIREAAG 400
    VREIPSDEQL KEWVDKCADC GACYLACPIE LDIPEAMKFA KQGDFSYLED 450
    LHDACIGCRR CEQVCKKEIP ILSVIEKASQ KIIAEEKGWM RAGRGQVSDA 500
    EIRAEGLNLV MGTTPGIIAI IGCPNYSDCA KAVYYIAEEF LKRNYIVVGT 550
    GCGSMDMGMY KDEDGKTLYE RFPGGFQSGG LVNIGSCVSN AHITGAAQKV 600
    AGIFGGRTME GNLAEIADYV LNRVGACGLA WGAFSQKASS IGTGCNIYGI 650
    PAVLGAHSSK YRRALIAKNY DESKWKVYDA RNGEEMPIPP APEFLLTTAE 700
    TWQEAIPMMA KACLRPSDNS LGRSIKLTHW MELHDKYIGG LPEDWWKFIR 750
    TEADLPLAKR ADLMKKLEAE RGWEIDWKKK KIISGPKIKF DVSAQPTNLK 800
    RLCKGA 806
    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

    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