PHAB_SYNY3
ID PHAB_SYNY3 Reviewed; 240 AA.
AC P73826;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Acetoacetyl-CoA reductase {ECO:0000303|PubMed:26358291};
DE EC=1.1.1.36 {ECO:0000305|PubMed:26358291};
GN Name=phaB {ECO:0000303|PubMed:11010896}; OrderedLocusNames=slr1994;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND EXPRESSION IN E.COLI.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=11010896; DOI=10.1128/aem.66.10.4440-4448.2000;
RA Taroncher-Oldenburg G., Nishina K., Stephanopoulos G.;
RT "Identification and analysis of the polyhydroxyalkanoate-specific beta-
RT ketothiolase and acetoacetyl coenzyme A reductase genes in the
RT cyanobacterium Synechocystis sp. strain PCC6803.";
RL Appl. Environ. Microbiol. 66:4440-4448(2000).
RN [3] {ECO:0007744|PDB:4RZI}
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS), FUNCTION, PATHWAY, ACTIVE SITE, AND
RP MUTAGENESIS OF SER-134; TYR-147 AND LYS-151.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=26358291; DOI=10.1016/j.febslet.2015.09.001;
RA Liu Y., Feng Y., Cao X., Li X., Xue S.;
RT "Structure-directed construction of a high-performance version of the
RT enzyme FabG from the photosynthetic microorganism Synechocystis sp. PCC
RT 6803.";
RL FEBS Lett. 589:3052-3057(2015).
CC -!- FUNCTION: Catalyzes the reduction of acetoacetyl-CoA to (R)-3-
CC hydroxybutyryl-CoA (PubMed:26358291). When expressed in E.coli with
CC Synechocystis PhaA, PhaC and PhaE confers the ability to synthesize up
CC to 12% (w/w) poly(3-hydroxybutyrate) (PHB) depending on the carbon
CC source (PubMed:11010896). {ECO:0000269|PubMed:11010896,
CC ECO:0000305|PubMed:26358291}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA + NADP(+) = a 3-oxoacyl-CoA + H(+) +
CC NADPH; Xref=Rhea:RHEA:22256, ChEBI:CHEBI:15378, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:90726; EC=1.1.1.36;
CC Evidence={ECO:0000305|PubMed:26358291};
CC -!- PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC biosynthesis. {ECO:0000269|PubMed:11010896}.
CC -!- DISRUPTION PHENOTYPE: Double deletion of phaA and phaB leads to loss of
CC synthesis of PHB, no visible growth phenotype.
CC {ECO:0000269|PubMed:11010896}.
CC -!- BIOTECHNOLOGY: Poly(3-hydroxyalkanoic acids) (PHA), of which PHB is
CC among the most common compounds, are prokaryotic intracellular storage
CC compounds with potential uses as a renewable, biodegradable
CC thermoplastic. Cyanobacterial PHB synthesis is particularly attractive
CC as cyanobacteria use CO(2) as the carbon source. {ECO:0000305}.
CC -!- MISCELLANEOUS: Nitrogen-free medium induces chlorosis in Synechocystis,
CC leading to the degradation of the photosynthetic apparatus and
CC concomitant accumulation of cytoplasmic polyhydroxyalkanoic acid (PHA)
CC granules which in this cyanobacterium are composed of PHB.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BA000022; BAA17883.1; -; Genomic_DNA.
DR PIR; S75021; S75021.
DR PDB; 4RZI; X-ray; 2.89 A; A/B/C=1-240.
DR PDBsum; 4RZI; -.
DR AlphaFoldDB; P73826; -.
DR SMR; P73826; -.
DR STRING; 1148.1652966; -.
DR PaxDb; P73826; -.
DR EnsemblBacteria; BAA17883; BAA17883; BAA17883.
DR KEGG; syn:slr1994; -.
DR eggNOG; COG1028; Bacteria.
DR InParanoid; P73826; -.
DR OMA; KGAFYCA; -.
DR PhylomeDB; P73826; -.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR GO; GO:0042619; P:poly-hydroxybutyrate biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; PHB biosynthesis; Reference proteome.
FT CHAIN 1..240
FT /note="Acetoacetyl-CoA reductase"
FT /id="PRO_0000054692"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001,
FT ECO:0000305|PubMed:26358291"
FT BINDING 18..20
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P14697"
FT BINDING 82..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P14697"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26358291"
FT BINDING 141..144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14697"
FT BINDING 177..180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P14697"
FT BINDING 178..179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14697"
FT MUTAGEN 134
FT /note="S->A: 12% enzymatic activity."
FT /evidence="ECO:0000269|PubMed:26358291"
FT MUTAGEN 147
FT /note="Y->A: No enzymatic activity."
FT /evidence="ECO:0000269|PubMed:26358291"
FT MUTAGEN 151
FT /note="K->A: 5% enzymatic activity."
FT /evidence="ECO:0000269|PubMed:26358291"
FT TURN 5..8
FT /evidence="ECO:0007829|PDB:4RZI"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:4RZI"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:4RZI"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:4RZI"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:4RZI"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4RZI"
FT HELIX 59..73
FT /evidence="ECO:0007829|PDB:4RZI"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4RZI"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4RZI"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:4RZI"
FT HELIX 108..124
FT /evidence="ECO:0007829|PDB:4RZI"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:4RZI"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:4RZI"
FT HELIX 145..165
FT /evidence="ECO:0007829|PDB:4RZI"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4RZI"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:4RZI"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4RZI"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:4RZI"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:4RZI"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:4RZI"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:4RZI"
SQ SEQUENCE 240 AA; 25333 MW; 7C2F8A33C434645F CRC64;
MLSLGLEDKV IVVTGGNRGI GAAIVKLLQE MGAKVAFTDL ATDGGNTEAL GVVANVTDLE
SMTAAAAEIT DKLGPVYGVV ANAGITKDNF FPKLTPADWD AVLNVNLKGV AYSIKPFIEG
MYERKAGSIV AISSISGERG NVGQTNYSAT KAGVIGMMKS LAREGARYGV RANAVAPGFI
DTEMTLAIRE DIREKITKEI PFRRFGKPEE IAWAVAFLLS PVASSYVTGE VLRVNGAHHT
