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Q07341

- ACSD_MOOTH

UniProt

Q07341 - ACSD_MOOTH

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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

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 oxygen

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
Complete GO annotation...

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 subunit
PRO_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

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni273 – 2786Cobalamin-binding Reviewed prediction

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

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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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531R → E AA sequence 1 Publication

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: June 11, 2014
This is version 69 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

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