Reviewed, UniProtKB/Swiss-Prot P45375 (PHBB_CHRVI)

Names and origin

Protein names

Recommended name:
    Acetoacetyl-CoA reductase
    EC=1.1.1.36

Gene names

Name:

phbB

Organism

Chromatium vinosum (Allochromatium vinosum)

Taxonomic identifier

1049 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Allochromatium

Protein attributes

Sequence length	246 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
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: 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 – 246	246	Acetoacetyl-CoA reductase		PRO_0000054749
Regions
	Nucleotide binding	7 – 31	25	NADP By similarity
Sites
	Active site	153	1	Proton acceptor By similarity
	Binding site	140	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45375-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 291E37450A1F54E9	FASTA	246	26,123
	10 20 30 40 50 60 MARIALVTGG IGGIGTSICT RLAKDGCTVV ANCHPSEAAA AEEWKQARAA EGFDIAVFTA 70 80 90 100 110 120 DVSSFDDSAR MVREITEQVG PIDILVNCAG ITRDKTFKKM EQAHWEAVIN VNLNSVFNVT 130 140 150 160 170 180 RQVWDGMLER GFGRIINISS VNGQRGQFGQ ANYSAAKAGM HGFTMALAQE GASKGVTVNT 190 200 210 220 230 240 ISPGYVETAM TLAMNDDVRN SIISGIPMRR MAQPNEIAAA IAFLAGDESG YMTGANLPVN GGLFMH

References

[1]

"Cloning and nucleotide sequences of genes relevant for biosynthesis of poly(3-hydroxybutyric acid) in Chromatium vinosum strain D." Liebergesell M., Steinbuechel A. Eur. J. Biochem. 209:135-150(1992) [PubMed: 1396692] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 17899 / DSM 180 / D.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L01112 Genomic DNA. Translation: AAA23325.1.
PIR	S29279.
3D structure databases
HSSP	HSSP built from PDB template 1FK8 based on UniProtKB Q9ZFY9.
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

PHBB_CHRVI

Accession

Primary (citable) accession number: P45375

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 25, 2008
This is version 53 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)