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Q07341 (ACSD_MOOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Corrinoid/iron-sulfur protein small subunit

Short name=C/Fe-SP small subunit
Short name=CFeSP small subunit
Gene names
Name:acsD
OrganismMoorella thermoacetica (Clostridium thermoaceticum)
Taxonomic identifier1525 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a methyl group carrier in the anaerobic acetyl-CoA pathway (Wood-Ljungdahl pathway) of carbon monoxide and carbon dioxide fixation. Ref.1 Ref.2 Ref.3

Subunit structure

Heterohexamer composed of 2 subunits of AcsC, 2 subunits of AcsD and 2 subunits of AcsE. Ref.3

Ontologies

Keywords
   Biological processCarbon dioxide fixation
   LigandCobalamin
Cobalt
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbon fixation

Inferred from direct assay Ref.3. Source: UniProtKB

one-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncobalamin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 323322Corrinoid/iron-sulfur protein small subunit
PRO_0000064443

Regions

Region273 – 2786Cobalamin-binding Potential

Sites

Binding site1881Cobalamin; via carbonyl oxygen

Experimental info

Sequence conflict531R → E AA sequence Ref.2

Secondary structure

................................................................ 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07341 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 51633BDB94036056

FASTA32335,070
        10         20         30         40         50         60 
MAVQILRDRS RAAVQKVVLG ATKDQGGTRS HTIVVGGDAA LPFHHFEGEI VNRPVIGMEV 

        70         80         90        100        110        120 
QDIVPDWPDV LKDPFTDVIN EPGRWAQKCV AEYGADLIYL KLDGADPEGA NHSVDQCVAT 

       130        140        150        160        170        180 
VKEVLQAVGV PLVVVGCGDV EKDHEVLEAV AEAAAGENLL LGNAEQENYK SLTAACMVHK 

       190        200        210        220        230        240 
HNIIARSPLD INICKQLNIL INEMNLPLDH IVIDPSIGGL GYGIEYSFSI MERIRLGALQ 

       250        260        270        280        290        300 
GDKMLSMPVI CTVGYEAWRA KEASAPVSEY PGWGKETERG ILWEAVTATA LLQAGAHILL 

       310        320 
MRHPEAVARV KENIDQLMVS NAY 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07100 Genomic DNA. Translation: AAA23255.1.
PIRB46621.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DJDX-ray2.38D/F1-323[»]
4DJEX-ray3.50D/F1-323[»]
4DJFX-ray3.03D/F1-323[»]
ProteinModelPortalQ07341.
SMRQ07341. Positions 3-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59670N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:COEALPHACLTH-MONOMER.

Family and domain databases

InterProIPR016041. Ac-CoA_synth_d_su_TIM-brl.
IPR004486. CO_DH/Ac-CoA_synth_dsu.
IPR011005. Dihydropteroate_synth-like.
[Graphical view]
PfamPF03599. CdhD. 1 hit.
[Graphical view]
SUPFAMSSF51717. SSF51717. 1 hit.
TIGRFAMsTIGR00381. cdhD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACSD_MOOTH
AccessionPrimary (citable) accession number: Q07341
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references