PHAJ_AERCA
ID PHAJ_AERCA Reviewed; 134 AA.
AC O32472;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=(R)-specific enoyl-CoA hydratase;
DE EC=4.2.1.119 {ECO:0000269|PubMed:9457873};
GN Name=phaJ;
OS Aeromonas caviae (Aeromonas punctata).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=648;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=FA440;
RX PubMed=9244271; DOI=10.1128/jb.179.15.4821-4830.1997;
RA Fukui T., Doi Y.;
RT "Cloning and analysis of the poly(3-hydroxybutyrate-co-3-hydroxyhexanoate)
RT biosynthesis genes of Aeromonas caviae.";
RL J. Bacteriol. 179:4821-4830(1997).
RN [2]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MASS
RP SPECTROMETRY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=FA440;
RX PubMed=9457873; DOI=10.1128/jb.180.3.667-673.1998;
RA Fukui T., Shiomi N., Doi Y.;
RT "Expression and characterization of (R)-specific enoyl coenzyme A hydratase
RT involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae.";
RL J. Bacteriol. 180:667-673(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), AND MUTAGENESIS OF ASP-32; HIS-37
RP AND SER-63.
RX PubMed=12409309; DOI=10.1074/jbc.m205484200;
RA Hisano T., Tsuge T., Fukui T., Iwata T., Miki K., Doi Y.;
RT "Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas
RT caviae involved in polyhydroxyalkanoate biosynthesis.";
RL J. Biol. Chem. 278:617-624(2003).
CC -!- FUNCTION: Catalyzes the hydration of trans-2-enoyl-CoA with a chain-
CC length of 4-6 carbon atoms, forming the corresponding (3R)-3-
CC hydroxyacyl-CoA. {ECO:0000269|PubMed:9244271,
CC ECO:0000269|PubMed:9457873}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26526, ChEBI:CHEBI:15377, ChEBI:CHEBI:57319,
CC ChEBI:CHEBI:58856; EC=4.2.1.119;
CC Evidence={ECO:0000269|PubMed:9457873};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=29 uM for crotonyl-CoA {ECO:0000269|PubMed:9457873};
CC KM=36 uM for 2-pentenoyl-CoA {ECO:0000269|PubMed:9457873};
CC KM=34 uM for 2-hexenoyl-CoA {ECO:0000269|PubMed:9457873};
CC KM=50 uM for 2-octenoyl-CoA {ECO:0000269|PubMed:9457873};
CC Vmax=6200 umol/min/mg enzyme with crotonyl-CoA as substrate
CC {ECO:0000269|PubMed:9457873};
CC Vmax=2800 umol/min/mg enzyme with 2-pentenoyl-CoA as substrate
CC {ECO:0000269|PubMed:9457873};
CC Vmax=1800 umol/min/mg enzyme with 2-hexenoyl-CoA as substrate
CC {ECO:0000269|PubMed:9457873};
CC Vmax=2.5 umol/min/mg enzyme with 2-octenoyl-CoA as substrate
CC {ECO:0000269|PubMed:9457873};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9457873}.
CC -!- MASS SPECTROMETRY: Mass=13963; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9457873};
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DR EMBL; D88825; BAA21816.1; -; Genomic_DNA.
DR PDB; 1IQ6; X-ray; 1.50 A; A/B=1-134.
DR PDBsum; 1IQ6; -.
DR AlphaFoldDB; O32472; -.
DR SMR; O32472; -.
DR KEGG; ag:BAA21816; -.
DR SABIO-RK; O32472; -.
DR EvolutionaryTrace; O32472; -.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SUPFAM; SSF54637; SSF54637; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Fatty acid metabolism;
KW Lipid metabolism; Lyase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9457873"
FT CHAIN 2..134
FT /note="(R)-specific enoyl-CoA hydratase"
FT /id="PRO_0000413682"
FT DOMAIN 5..119
FT /note="MaoC-like"
FT BINDING 32..37
FT /ligand="a (3R)-3-hydroxyacyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57319"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="a (3R)-3-hydroxyacyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57319"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="a (3R)-3-hydroxyacyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57319"
FT /evidence="ECO:0000250"
FT MUTAGEN 32
FT /note="D->A: Almost no activity."
FT /evidence="ECO:0000269|PubMed:12409309"
FT MUTAGEN 37
FT /note="H->A,N: Almost no activity."
FT /evidence="ECO:0000269|PubMed:12409309"
FT MUTAGEN 63
FT /note="S->A: 100-fold lower Vmax."
FT /evidence="ECO:0000269|PubMed:12409309"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:1IQ6"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:1IQ6"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1IQ6"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1IQ6"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:1IQ6"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1IQ6"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:1IQ6"
FT STRAND 105..117
FT /evidence="ECO:0007829|PDB:1IQ6"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:1IQ6"
SQ SEQUENCE 134 AA; 14086 MW; ECB87170A10A2C9F CRC64;
MSAQSLEVGQ KARLSKRFGA AEVAAFAALS EDFNPLHLDP AFAATTAFER PIVHGMLLAS
LFSGLLGQQL PGKGSIYLGQ SLSFKLPVFV GDEVTAEVEV TALREDKPIA TLTTRIFTQG
GALAVTGEAV VKLP
