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Q975C8 (ACAR_SULTO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acryloyl-coenzyme A reductase
Short name=Acryloyl-CoA reductase
EC=1.3.1.84
Gene names
Ordered Locus Names:STK_04800
OrganismSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) [Complete proteome] [HAMAP]
Taxonomic identifier273063 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus ›

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the acryloyl-CoA dependent NADPH oxidation and formation of propionyl-CoA. Inactive towards 3-hydroxypropionyl-CoA, NADH and crotonyl-CoA. Ref.2

Catalytic activity

Propanoyl-CoA + NADP+ = acrylyl-CoA + NADPH. Ref.2

Cofactor

Zinc. Ref.2

Subunit structure

Monomer. Ref.2

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=36 µM for NADPH Ref.2

KM=3 µM for acryloyl-CoA Ref.2

pH dependence:

Optimum pH is 6.0 at 65 degrees Celsius. Retains half maximum activity at pH 7.5 at 65 degrees Celsius. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Acryloyl-coenzyme A reductase
PRO_0000404602

Regions

Nucleotide binding173 – 1764NADP By similarity
Nucleotide binding195 – 1973NADP By similarity

Sites

Metal binding381Zinc 1; catalytic By similarity UniProtKB P39462
Metal binding601Zinc 1; catalytic By similarity UniProtKB P39462
Metal binding901Zinc 2 By similarity UniProtKB P39462
Metal binding931Zinc 2 By similarity UniProtKB P39462
Metal binding961Zinc 2 By similarity UniProtKB P39462
Metal binding1041Zinc 2 By similarity UniProtKB P39462
Metal binding1461Zinc 1; catalytic By similarity UniProtKB P39462
Binding site391NADP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q975C8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 6CA4998B7EAE4D95

FASTA33436,300
        10         20         30         40         50         60 
MKAIVVPGPK QGYKLEEVPD PKPGKDEVII RVDRAALCYR DLLQLQGYYP RMKYPVILGH 

        70         80         90        100        110        120 
EVVGTIEEVG ENIKGFEVGD KVISLLYAPD GTCEYCQIGE EAYCHHRLGY SEELDGFFAE 

       130        140        150        160        170        180 
KAKIKVTSLV KVPKGTPDEG AVLVPCVTGM IYRGIRRAGG IRKGELVLVT GASGGVGIHA 

       190        200        210        220        230        240 
IQVAKALGAK VIGVTTSEEK AKIIKQYADY VIVGTKFSEE AKKIGDVTLV IDTVGTPTFD 

       250        260        270        280        290        300 
ESLKSLWMGG RIVQIGNVDP SQIYNLRLGY IILKDLKIVG HASATKKDAE DTLKLTQEGK 

       310        320        330 
IKPVIAGTVS LENIDEGYKM IKDKNKVGKV LVKP

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7."
Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.
DNA Res. 8:123-140(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.
[2]"3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales."
Teufel R., Kung J.W., Kockelkorn D., Alber B.E., Fuchs G.
J. Bacteriol. 191:4572-4581(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000023 Genomic DNA. Translation: BAB65473.1.
FJ445417 Genomic DNA. Translation: ACJ71675.1.
RefSeqNP_376364.1. NC_003106.2.

3D structure databases

HSSPHSSP built from PDB template 1F8F based on UniProtKB Q59096.
ProteinModelPortalQ975C8.
ModBaseSearch...

Protein-protein interaction databases

STRING273063.ST0480.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB65473; BAB65473; STK_04800.
GeneID1458422.
KEGGsto:ST0480.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1064.
HOGENOMHOG000294685.
KOK15020.
OMAHSVRIAN.
ProtClustDBPRK13771.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13730.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR002364. Quin_OxRdtase/zeta-crystal_CS.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
PS01162. QOR_ZETA_CRYSTAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACAR_SULTO
AccessionPrimary (citable) accession number: Q975C8
Secondary accession number(s): B8XVT1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: December 1, 2001
Last modified: May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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