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Q07341

- ACSD_MOOTH

UniProt

Q07341 - ACSD_MOOTH

Protein

Corrinoid/iron-sulfur protein small subunit

Gene

acsD

Organism
Moorella thermoacetica (Clostridium thermoaceticum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Acts as a methyl group carrier in the anaerobic acetyl-CoA pathway (Wood-Ljungdahl pathway) of carbon monoxide and carbon dioxide fixation.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei188 – 1881Cobalamin; via carbonyl oxygen1 Publication

    GO - Molecular functioni

    1. cobalamin binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. carbon fixation Source: UniProtKB
    2. one-carbon metabolic process Source: InterPro

    Keywords - Biological processi

    Carbon dioxide fixation

    Keywords - Ligandi

    Cobalamin, Cobalt

    Enzyme and pathway databases

    BioCyciMetaCyc:COEALPHACLTH-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Corrinoid/iron-sulfur protein small subunit
    Short name:
    C/Fe-SP small subunit
    Short name:
    CFeSP small subunit
    Gene namesi
    Name:acsD
    OrganismiMoorella thermoacetica (Clostridium thermoaceticum)
    Taxonomic identifieri1525 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 323322Corrinoid/iron-sulfur protein small subunitPRO_0000064443Add
    BLAST

    Interactioni

    Subunit structurei

    Heterohexamer composed of 2 subunits of AcsC, 2 subunits of AcsD and 2 subunits of AcsE.1 Publication

    Protein-protein interaction databases

    DIPiDIP-59670N.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 194
    Helixi23 – 253
    Beta strandi33 – 364
    Helixi45 – 473
    Beta strandi55 – 639
    Helixi69 – 724
    Helixi73 – 753
    Turni76 – 805
    Helixi82 – 9110
    Beta strandi96 – 1016
    Helixi103 – 1053
    Turni107 – 1104
    Helixi114 – 12714
    Beta strandi132 – 1354
    Helixi140 – 15314
    Turni154 – 1563
    Beta strandi160 – 1656
    Beta strandi166 – 1683
    Helixi170 – 17910
    Beta strandi182 – 1865
    Helixi191 – 20212
    Turni203 – 2053
    Helixi208 – 2103
    Beta strandi211 – 2144
    Turni220 – 2234
    Helixi224 – 24017
    Helixi243 – 2453
    Beta strandi249 – 2524
    Helixi253 – 2586
    Helixi261 – 2644
    Turni267 – 2693
    Helixi271 – 2733
    Helixi276 – 29217
    Turni293 – 2953
    Beta strandi297 – 3015
    Helixi304 – 31714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DJDX-ray2.38D/F1-323[»]
    4DJEX-ray3.50D/F1-323[»]
    4DJFX-ray3.03D/F1-323[»]
    ProteinModelPortaliQ07341.
    SMRiQ07341. Positions 3-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni273 – 2786Cobalamin-bindingSequence Analysis

    Family and domain databases

    InterProiIPR016041. Ac-CoA_synth_d_su_TIM-brl.
    IPR004486. CO_DH/Ac-CoA_synth_dsu.
    IPR011005. Dihydropteroate_synth-like.
    [Graphical view]
    PfamiPF03599. CdhD. 1 hit.
    [Graphical view]
    SUPFAMiSSF51717. SSF51717. 1 hit.
    TIGRFAMsiTIGR00381. cdhD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q07341-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVQILRDRS RAAVQKVVLG ATKDQGGTRS HTIVVGGDAA LPFHHFEGEI    50
    VNRPVIGMEV QDIVPDWPDV LKDPFTDVIN EPGRWAQKCV AEYGADLIYL 100
    KLDGADPEGA NHSVDQCVAT VKEVLQAVGV PLVVVGCGDV EKDHEVLEAV 150
    AEAAAGENLL LGNAEQENYK SLTAACMVHK HNIIARSPLD INICKQLNIL 200
    INEMNLPLDH IVIDPSIGGL GYGIEYSFSI MERIRLGALQ GDKMLSMPVI 250
    CTVGYEAWRA KEASAPVSEY PGWGKETERG ILWEAVTATA LLQAGAHILL 300
    MRHPEAVARV KENIDQLMVS NAY 323
    Length:323
    Mass (Da):35,070
    Last modified:January 23, 2007 - v2
    Checksum:i51633BDB94036056
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531R → E AA sequence (PubMed:2911576)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07100 Genomic DNA. Translation: AAA23255.1.
    PIRiB46621.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07100 Genomic DNA. Translation: AAA23255.1 .
    PIRi B46621.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DJD X-ray 2.38 D/F 1-323 [» ]
    4DJE X-ray 3.50 D/F 1-323 [» ]
    4DJF X-ray 3.03 D/F 1-323 [» ]
    ProteinModelPortali Q07341.
    SMRi Q07341. Positions 3-318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59670N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:COEALPHACLTH-MONOMER.

    Family and domain databases

    InterProi IPR016041. Ac-CoA_synth_d_su_TIM-brl.
    IPR004486. CO_DH/Ac-CoA_synth_dsu.
    IPR011005. Dihydropteroate_synth-like.
    [Graphical view ]
    Pfami PF03599. CdhD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51717. SSF51717. 1 hit.
    TIGRFAMsi TIGR00381. cdhD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and expression of the gene encoding the corrinoid/iron-sulfur protein from Clostridium thermoaceticum and reconstitution of the recombinant protein to full activity."
      Lu W.-P., Schiau I., Cunningham J.R., Ragsdale S.W.
      J. Biol. Chem. 268:5605-5614(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
    2. "Cloning and expression of the gene cluster encoding key proteins involved in acetyl-CoA synthesis in Clostridium thermoaceticum: CO dehydrogenase, the corrinoid/Fe-S protein, and methyltransferase."
      Roberts D.L., James-Hagstrom J.E., Garvin D.K., Gorst C.M., Runquist J.A., Baur J.R., Haase F.C., Ragsdale S.W.
      Proc. Natl. Acad. Sci. U.S.A. 86:32-36(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-53, PROTEIN SEQUENCE OF 30-63, FUNCTION.
      Strain: DSM 521.
    3. "Visualizing molecular juggling within a B12-dependent methyltransferase complex."
      Kung Y., Ando N., Doukov T.I., Blasiak L.C., Bender G., Seravalli J., Ragsdale S.W., Drennan C.L.
      Nature 484:265-269(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH ACSC; ACSE AND COBALAMIN, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiACSD_MOOTH
    AccessioniPrimary (citable) accession number: Q07341
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 70 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3