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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: 3 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 oxygen1 Publication

GO - Molecular functioni

  1. cobalamin binding Source: UniProtKB-KW

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 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 – 194Combined sources
Helixi23 – 253Combined sources
Beta strandi33 – 364Combined sources
Helixi45 – 473Combined sources
Beta strandi55 – 639Combined sources
Helixi69 – 724Combined sources
Helixi73 – 753Combined sources
Turni76 – 805Combined sources
Helixi82 – 9110Combined sources
Beta strandi96 – 1016Combined sources
Helixi103 – 1053Combined sources
Turni107 – 1104Combined sources
Helixi114 – 12714Combined sources
Beta strandi132 – 1354Combined sources
Helixi140 – 15314Combined sources
Turni154 – 1563Combined sources
Beta strandi160 – 1656Combined sources
Beta strandi166 – 1683Combined sources
Helixi170 – 17910Combined sources
Beta strandi182 – 1865Combined sources
Helixi191 – 20212Combined sources
Turni203 – 2053Combined sources
Helixi208 – 2103Combined sources
Beta strandi211 – 2144Combined sources
Turni220 – 2234Combined sources
Helixi224 – 24017Combined sources
Helixi243 – 2453Combined sources
Beta strandi249 – 2524Combined sources
Helixi253 – 2586Combined sources
Helixi261 – 2644Combined sources
Turni267 – 2693Combined sources
Helixi271 – 2733Combined sources
Helixi276 – 29217Combined sources
Turni293 – 2953Combined sources
Beta strandi297 – 3015Combined sources
Helixi304 – 31714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MAVQILRDRS RAAVQKVVLG ATKDQGGTRS HTIVVGGDAA LPFHHFEGEI
60 70 80 90 100
VNRPVIGMEV QDIVPDWPDV LKDPFTDVIN EPGRWAQKCV AEYGADLIYL
110 120 130 140 150
KLDGADPEGA NHSVDQCVAT VKEVLQAVGV PLVVVGCGDV EKDHEVLEAV
160 170 180 190 200
AEAAAGENLL LGNAEQENYK SLTAACMVHK HNIIARSPLD INICKQLNIL
210 220 230 240 250
INEMNLPLDH IVIDPSIGGL GYGIEYSFSI MERIRLGALQ GDKMLSMPVI
260 270 280 290 300
CTVGYEAWRA KEASAPVSEY PGWGKETERG ILWEAVTATA LLQAGAHILL
310 320
MRHPEAVARV KENIDQLMVS NAY
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:
EMBLi
GenBanki
DDBJi
Links Updated
L07100 Genomic DNA. Translation: AAA23255.1.
PIRiB46621.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07100 Genomic DNA. Translation: AAA23255.1 .
PIRi B46621.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 72 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