Q07341 (ACSD_MOOTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Corrinoid/iron-sulfur protein small subunit

Alternative name(s):
C/Fe-SP

Gene names

Name:

acsD

Organism

Moorella thermoacetica (Clostridium thermoaceticum)

Taxonomic identifier

1525 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteraceae › Moorella group › Moorella

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Subunit structure	Heterodimer of a large and a small chain.

Ontologies

Keywords
Biological process	Carbon dioxide fixation
Ligand	Cobalamin Cobalt
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbon fixation Inferred from electronic annotation. Source: UniProtKB-KW one-carbon metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	cobalamin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 323

322

Corrinoid/iron-sulfur protein small subunit

PRO_0000064443

Regions

Region

273 – 278

6

Cobalamin-binding Potential

Experimental info

Sequence conflict

53

1

R → E AA sequence Ref.2

Secondary structure

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323

Helix Strand Turn

Details...

Beta strand

16 – 19

4

Helix

23 – 25

3

Beta strand

33 – 36

4

Helix

45 – 47

3

Beta strand

55 – 63

9

Helix

69 – 72

4

Helix

73 – 75

3

Turn

76 – 80

5

Helix

82 – 91

10

Beta strand

96 – 101

6

Helix

103 – 105

3

Turn

107 – 110

4

Helix

114 – 127

14

Beta strand

132 – 135

4

Helix

140 – 153

14

Turn

154 – 156

3

Beta strand

160 – 165

6

Beta strand

166 – 168

3

Helix

170 – 179

10

Beta strand

182 – 186

5

Helix

191 – 202

12

Turn

203 – 205

3

Helix

208 – 210

3

Beta strand

211 – 214

4

Turn

220 – 223

4

Helix

224 – 240

17

Helix

243 – 245

3

Beta strand

249 – 252

4

Helix

253 – 258

6

Helix

261 – 264

4

Turn

267 – 269

3

Helix

271 – 273

3

Helix

276 – 292

17

Turn

293 – 295

3

Beta strand

297 – 301

5

Helix

304 – 317

14

Sequences

	Sequence		Length	Mass (Da)
	Q07341 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 51633BDB94036056	FASTA	323	35,070
	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

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.
[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. Strain: DSM 521.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L07100 Genomic DNA. Translation: AAA23255.1.

PIR

B46621.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q07341.

SMR

Q07341. Positions 3-318.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59670N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:COEALPHACLTH-MONOMER.

Family and domain databases

InterPro

IPR016041. Ac-CoA_synth_d_su_TIM-brl.
IPR004486. CO_DH/Ac-CoA_synth_dsu.
IPR011005. Dihydropteroate_synth-like.
[Graphical view]

Pfam

PF03599. CdhD. 1 hit.
[Graphical view]

SUPFAM

SSF51717. DHP_synth_like. 1 hit.

TIGRFAMs

TIGR00381. cdhD. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ACSD_MOOTH

Accession

Primary (citable) accession number: Q07341

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program