P50204 (PHAB_PARDE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetoacetyl-CoA reductase
EC=1.1.1.36

Gene names

Name:

phaB

Organism

Paracoccus denitrificans

Taxonomic identifier

266 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length	242 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH.
Pathway	Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis.
Subcellular location	Cytoplasm.
Miscellaneous	NADH was preferred to NADPH as a substrate.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	PHB biosynthesis
Cellular component	Cytoplasm
Ligand	NAD NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	poly-hydroxybutyrate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetoacetyl-CoA reductase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 242	242	Acetoacetyl-CoA reductase		PRO_0000054747
Regions
	Nucleotide binding	7 – 31	25	NAD By similarity
Sites
	Active site	147	1	Proton acceptor By similarity
	Binding site	134	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50204 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 3CD4B9BD23FC98FD	FASTA	242	25,615
	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

References

[1]	"Analysis of beta-ketothiolase and acetoacetyl-CoA reductase genes of a methylotrophic bacterium, Paracoccus denitrificans, and their expression in Escherichia coli." Yabutani T., Maehara A., Ueda S., Yamane T. FEMS Microbiol. Lett. 133:85-90(1995) [PubMed: 8566717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D49362 Genomic DNA. Translation: BAA08358.1.
3D structure databases
ProteinModelPortal	P50204.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR011283. Acetoacetyl-CoA_reductase. IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
TIGRFAMs	TIGR01829. AcAcCoA_reduct. 1 hit.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHAB_PARDE

Accession

Primary (citable) accession number: P50204

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program