[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=7635832 [NCBI, ExPASy, EBI, Israel, Japan] Schembri M.A., Bayly R.C., Davies J.K.; "Phosphate concentration regulates transcription of the Acinetobacter polyhydroxyalkanoic acid biosynthetic genes."; J. Bacteriol. 177:4501-4507(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.
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

L37761; AAA99472.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q01782; 1E7W. [HSSP ENTRY / PDB]

ModBase

P50203.

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

P50203.

UniRef

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

Keywords

Cytoplasm; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 248`	`248`	`Acetoacetyl-CoA reductase.`	`PRO_0000054746`
`NP_BIND`	`9 33`	`25`	`NADP (By similarity).`
`ACT_SITE`	`155 155`		`Proton acceptor (By similarity).`
`BINDING`	`142 142`		`Substrate (By similarity).`

Sequence information

Length: 248 AA [This is the length of the unprocessed precursor]

Molecular weight: 26727 Da [This is the MW of the unprocessed precursor]

CRC64: 850E0DC659795123 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEQKVALVT GALGGIGSEI CRQLVTAGYK IIATVVPREE DREKQWLQSE GFQDSDVRFV 

        70         80         90        100        110        120 
LTDLNNHEAA TAAIQEAIAA EGRVDVLVNN AGITRDATFK KMSYEQWSQV IDTNLKTLFT 

       130        140        150        160        170        180 
VTQPVFNKML EQKSGRIVNI SSVNGLKGQF GQANYSASKA GIIGFTKALA QEGARSNICV 

       190        200        210        220        230        240 
NVVAPGYTAT PMVTAMREDV IKSIEAQIPL QRLAAPAEIA AAVMYLVSEH GAYVTGETLS 


INGGLYMH

P50203 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