Reviewed, UniProtKB/Swiss-Prot P23238 (PHBB_ZOORA)

Names and origin

Protein names

Recommended name:
    Acetoacetyl-CoA reductase
    EC=1.1.1.36

Gene names

Name:

phbB

Organism

Zoogloea ramigera

Taxonomic identifier

350 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Zoogloea

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	PHB biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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 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 – 241	241	Acetoacetyl-CoA reductase		PRO_0000054751
Regions
	Nucleotide binding	7 – 31	25	NADP By similarity
Sites
	Active site	147	1	Proton acceptor By similarity
	Binding site	134	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23238-1 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 8FDD489C0D816804	FASTA	241	25,285
	10 20 30 40 50 60 MSRVALVTGG SRGIGAAISI ALKAAGYKVA ASYAGNDDAA KPFKAETGIA VYKWDVSSYE 70 80 90 100 110 120 ACVEGIAKVE ADLGPIDVLV NNAGITKDAM FHKMTPDQWN AVINTNLTGL FNMTHPVWSG 130 140 150 160 170 180 MRDRSFGRIV NISSINGQKG QMGQANYSAA KAGDLGFTKA LAQEGAAKGI TVNAICPGYI 190 200 210 220 230 240 GTEMVRAIPE KVLNERIIPQ IPVGRLGEPD EIARIVVFLA SDEAGFITGS TISANGGQFF V

References

[1]	"Fine structural analysis of the Zoogloea ramigera phbA-phbB locus encoding beta-ketothiolase and acetoacetyl-CoA reductase: nucleotide sequence of phbB." Peoples O.P., Sinskey A.J. Mol. Microbiol. 3:349-357(1989) [PubMed: 2546004] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 19623 / I-16-M / NCIB 10340 / NCTC 10482.
[2]	"The NADPH-linked acetoacetyl-CoA reductase from Zoogloea ramigera. Characterization and mechanistic studies of the cloned enzyme over-produced in Escherichia coli." Ploux O., Masamune S., Walsh C.T. Eur. J. Biochem. 174:177-182(1988) [PubMed: 3286259] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-31.

Cross-references

Sequence databases
PIR	S06998.
3D structure databases
HSSP	HSSP built from PDB template 1G0N based on UniProtKB Q12634.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MON-13089.
BRENDA	1.1.1.36. 341.
Family and domain databases
InterPro	IPR011283. Acetoacetyl-CoA_reductase. IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR19410. ADH_short_C2. 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

PHBB_ZOORA

Accession

Primary (citable) accession number: P23238

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	September 22, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)