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Protein

Corrinoid/iron-sulfur protein small subunit

Gene

acsD

Organism
Moorella thermoacetica (Clostridium thermoaceticum)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei188Cobalamin; via carbonyl oxygen1 Publication1

GO - Molecular functioni

GO - Biological processi

  • carbon fixation Source: UniProtKB
  • 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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000644432 – 323Corrinoid/iron-sulfur protein small subunitAdd BLAST322

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.
STRINGi264732.Moth_1198.

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 19Combined sources4
Helixi23 – 25Combined sources3
Beta strandi33 – 36Combined sources4
Helixi45 – 47Combined sources3
Beta strandi55 – 63Combined sources9
Helixi69 – 72Combined sources4
Helixi73 – 75Combined sources3
Turni76 – 80Combined sources5
Helixi82 – 91Combined sources10
Beta strandi96 – 101Combined sources6
Helixi103 – 105Combined sources3
Turni107 – 110Combined sources4
Helixi114 – 127Combined sources14
Beta strandi132 – 135Combined sources4
Helixi140 – 153Combined sources14
Turni154 – 156Combined sources3
Beta strandi160 – 165Combined sources6
Beta strandi166 – 168Combined sources3
Helixi170 – 179Combined sources10
Beta strandi182 – 186Combined sources5
Helixi191 – 202Combined sources12
Turni203 – 205Combined sources3
Helixi208 – 210Combined sources3
Beta strandi211 – 214Combined sources4
Turni220 – 223Combined sources4
Helixi224 – 240Combined sources17
Helixi243 – 245Combined sources3
Beta strandi249 – 252Combined sources4
Helixi253 – 258Combined sources6
Helixi261 – 264Combined sources4
Turni267 – 269Combined sources3
Helixi271 – 273Combined sources3
Helixi276 – 292Combined sources17
Turni293 – 295Combined sources3
Beta strandi297 – 301Combined sources5
Helixi304 – 317Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DJDX-ray2.38D/F1-323[»]
4DJEX-ray3.50D/F1-323[»]
4DJFX-ray3.03D/F1-323[»]
ProteinModelPortaliQ07341.
SMRiQ07341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni273 – 278Cobalamin-bindingSequence analysis6

Phylogenomic databases

eggNOGiENOG4106HYN. Bacteria.
COG2069. LUCA.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR016041. Ac-CoA_synth_d_su_TIM-brl.
IPR013785. Aldolase_TIM.
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)DescriptionActionsGraphical viewLength
Sequence conflicti53R → E AA sequence (PubMed:2911576).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07100 Genomic DNA. Translation: AAA23255.1.
PIRiB46621.
RefSeqiWP_011392712.1. NZ_CP012370.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07100 Genomic DNA. Translation: AAA23255.1.
PIRiB46621.
RefSeqiWP_011392712.1. NZ_CP012370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DJDX-ray2.38D/F1-323[»]
4DJEX-ray3.50D/F1-323[»]
4DJFX-ray3.03D/F1-323[»]
ProteinModelPortaliQ07341.
SMRiQ07341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59670N.
STRINGi264732.Moth_1198.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4106HYN. Bacteria.
COG2069. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:COEALPHACLTH-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR016041. Ac-CoA_synth_d_su_TIM-brl.
IPR013785. Aldolase_TIM.
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.
ProtoNetiSearch...

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 30, 2016
This is version 80 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.