Acetyl-CoA decarbonylase/synthase complex subunit gamma - Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

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O29871 (ACDG_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 67. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acetyl-CoA decarbonylase/synthase complex subunit gamma
Short name=ACDS complex subunit gamma
EC=2.1.1.-

Alternative name(s):
ACDS complex methyltransferase
Corrinoid/iron-sulfur component large subunit

Gene names

Name:	cdhE
Ordered Locus Names:	AF_0376

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

Taxonomic identifier

224325 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO₂ By similarity. HAMAP MF_01136
Catalytic activity	Cob(I)amide-protein + CH(3)-H₄SPt + H⁺ = CH(3)-cob(III)amide-protein + H₄SPt. HAMAP MF_01136
Cofactor	Corrinoid Probable. Binds 1 4Fe-4S cluster Probable.
Subunit structure	Heterodimer of delta and gamma chains. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha₂epsilon₂)(4)-beta(8)-(gamma₁delta₁)₈ Potential.
Sequence similarities	Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
Ligand	4Fe-4S Cobalt Iron Iron-sulfur Metal-binding
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	acetyl-CoA catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: InterPro methyltransferase activity 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

Chain

1 – 470

470

Acetyl-CoA decarbonylase/synthase complex subunit gamma HAMAP MF_01136

PRO_0000155118

Sites

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O29871 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 0BEC4537F265CA3A
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FASTA

470

52,551

        10         20         30         40         50         60 
MKVKSPLEVY NYLPRTNCGE CGFDTCMSFA AHILDRSVTP LDCKPLVRDA EKDPKVKKKL 

        70         80         90        100        110        120 
EELLELTAPE IAEVVIGVGE NAVKIGGEEV LHRHELTFFN PTGFFYDVWD TMDDKALEER 

       130        140        150        160        170        180 
CDRVVSYKKF YVGNFLTLDG FAVRCTSGDP KRYREVVKKV ASYGKPLILV ALDSECMKAA 

       190        200        210        220        230        240 
LEEVADQRPL MYAATEGNWK EFLKLALEYK VPVTLRAKDL DLLKSMAVTF KQAGVKDIVL 

       250        260        270        280        290        300 
DPVTEPLGEG LKGTFERVIQ LRRTAIAGQD KDVAYPIMIT PIAAWLIEGD DVTKSYWEAV 

       310        320        330        340        350        360 
IASIFIVKYG DVMIFRSIDQ HVVMPTITLR FNIYTDPRTP VQVEPGLRAI NDPGPDDPVF 

       370        380        390        400        410        420 
ITTNFALTYY TVESDLTSGG IKGWLLVLNT EGLGVEVSVA GGQFTASKVK ELIEETKIEE 

       430        440        450        460        470 
KVNHRYLVIP GLAARLQGAI EDETGWKVLV GPMDSGRIKG WLEKNWPPKE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. Venter J.C. Nature 390:364-370(1997) [PubMed: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]	"Acetyl-CoA decarbonylase/synthase complex from Archaeoglobus fulgidus." Dai Y.R., Reed D.W., Millstein J.H., Hartzell P.L., Grahame D.A., DeMoll E. Arch. Microbiol. 169:525-529(1998) [PubMed: 9575239] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-19. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000782 Genomic DNA. Translation: AAB90860.1.
PIR	H69296.
RefSeq	NP_069212.1. NC_000917.1.
3D structure databases
ProteinModelPortal	O29871.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1483591.
GenomeReviews	Gene locus AF_0376 in contig AE000782_GR.
KEGG	afu:AF0376.
NMPDR	fig\|224325.1.peg.371.
TIGR	AF_0376.
Phylogenomic databases
HOGENOM	HBG304431.
OMA	YTDPRKP.
ProtClustDB	PRK04165.
Enzyme and pathway databases
BioCyc	AFUL224325:AF_0376-MONOMER.
Family and domain databases
HAMAP	MF_01136. CdhE. [Tree]
InterPro	IPR016041. Ac-CoA_synth_d_su_TIM-brl. IPR016218. AcylCoA_decarb/synth_gsu. IPR023427. AcylCoA_decarb/synth_gsu_arc. IPR011005. Dihydropteroate_synth-like. IPR007202. FeS. [Graphical view]
KO	K00197.
Pfam	PF03599. CdhD. 1 hit. PF04060. FeS. 1 hit. [Graphical view]
PIRSF	PIRSF000376. AcCoA_decarb_gamma. 1 hit.
SUPFAM	SSF51717. DHP_synth_like. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACDG_ARCFU

Accession

Primary (citable) accession number: O29871

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 21, 2003
Last sequence update:	January 1, 1998
Last modified:	November 16, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents