Reviewed, UniProtKB/Swiss-Prot P50203 (PHAB_ACISR)

Names and origin

Protein names

Recommended name:
    Acetoacetyl-CoA reductase
    EC=1.1.1.36

Gene names

Name:

phaB

Organism

Acinetobacter sp. (strain RA3849)

Taxonomic identifier

68994 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	248 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-hydroxybutyric acid biosynthesis.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	acetoacetyl-CoA reductase activity Inferred from electronic annotation. Source: InterPro 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 – 248	248	Acetoacetyl-CoA reductase		PRO_0000054746
Regions
	Nucleotide binding	9 – 33	25	NADP By similarity
Sites
	Active site	155	1	Proton acceptor By similarity
	Binding site	142	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50203-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 850E0DC659795123	FASTA	248	26,727
	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

References

[1]	"Phosphate concentration regulates transcription of the Acinetobacter polyhydroxyalkanoic acid biosynthetic genes." Schembri M.A., Bayly R.C., Davies J.K. J. Bacteriol. 177:4501-4507(1995) [PubMed: 7635832] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	L37761 Genomic DNA. Translation: AAA99472.1.
3D structure databases
HSSP	HSSP built from PDB template 1E7W based on UniProtKB Q01782.
ModBase	Search...
Family and domain databases
InterPro	IPR011283. Acetoacetyl-CoA_reductase. IPR002198. DHase_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DHase. IPR016040. NAD(P)-bd. [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

PHAB_ACISR

Accession

Primary (citable) accession number: P50203

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 45 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)