NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1097(95)00341-2; PubMed=8566717 [NCBI, ExPASy, EBI, Israel, Japan]
Yabutani T., Maehara A., Ueda S., Yamane T.;
"Analysis of beta-ketothiolase and acetoacetyl-CoA reductase genes of a methylotrophic bacterium, Paracoccus denitrificans, and their expression in Escherichia coli.";
FEMS Microbiol. Lett. 133:85-90(1995).

Comments

CATALYTIC ACTIVITY: (R)-3-hydroxyacyl-CoA + NADP⁺ = 3-oxoacyl-CoA + NADPH.
PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutyric acid biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: NADH was preferred to NADPH as a substrate.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D49362; BAA08358.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q93X62; 1EDO. [HSSP ENTRY / PDB]

ModBase

P50204.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0018454;	Molecular function: acetoacetyl-CoA reductase activity (inferred from electronic annotation from InterPro).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0042619;	Biological process: poly-hydroxybutyrate biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR011283; Acetoacetyl-CoA_reductase.
IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

TIGRFAMs

TIGR01829; AcAcCoA_reduct; 1.

PROSITE

PS00061; ADH_SHORT; 1.

Other

ProtoNet

P50204.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; NAD; NADP; Oxidoreductase; PHB biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 242`	`242`	`Acetoacetyl-CoA reductase.`	`PRO_0000054747`
`NP_BIND`	`7 31`	`25`	`NAD (By similarity).`
`ACT_SITE`	`147 147`		`Proton acceptor (By similarity).`
`BINDING`	`134 134`		`Substrate (By similarity).`

Sequence information

Length: 242 AA [This is the length of the unprocessed precursor]

Molecular weight: 25615 Da [This is the MW of the unprocessed precursor]

CRC64: 3CD4B9BD23FC98FD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKVALVTGG SRGIGAAISK ALKEAGYTVA ANYAGNDDAA RAFTEETGIK TYKWSVADYD 

        70         80         90        100        110        120 
ACAAGIKQVE EELGPIAVLV NNAGITRDAM FHKMTPQQWK EVIDTNLTGL FNMTHPVWSG 

       130        140        150        160        170        180 
MRDRKYGRIV NISSINGQKG QAGQANYSAA KAGDLGFTKA LAQEGARAGI TVNAICPGYI 

       190        200        210        220        230        240 
GTEMVRAIDE KVLNEGIIPQ IPVAAWAEPE EIARCVVFLA SEDAGFITGS THQAPNGGQF 


FV

P50204 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools