PHAJ_RHORT
ID PHAJ_RHORT Reviewed; 144 AA.
AC Q2RQ36; Q9L9X2;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=(R)-specific enoyl-CoA hydratase;
DE EC=4.2.1.119 {ECO:0000269|PubMed:10709984};
DE AltName: Full=(R)-specific trans-2,3-enoylacyl-CoA hydratase {ECO:0000303|PubMed:10709984};
GN Name=phaJ {ECO:0000303|PubMed:10709984};
GN OrderedLocusNames=Rru_A2964 {ECO:0000312|EMBL:ABC23759.1};
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20 AND 78-91,
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=S1 / ATCC 25903 / S1H;
RX PubMed=10709984; DOI=10.1007/s002530050010;
RA Reiser S.E., Mitsky T.A., Gruys K.J.;
RT "Characterization and cloning of an (R)-specific trans-2,3-enoylacyl-CoA
RT hydratase from Rhodospirillum rubrum and use of this enzyme for PHA
RT production in Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 53:209-218(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
CC -!- FUNCTION: Catalyzes the hydration of trans-2-enoyl-CoAs with a chain-
CC length of 4-6 carbon atoms, forming the corresponding (3R)-3-
CC hydroxyacyl-CoAs, which can then be utilized for the production of
CC polyhydroxyalkanoates (PHA) polymers. Cannot use trans-2,3-octenoyl-CoA
CC as substrate. {ECO:0000269|PubMed:10709984}.
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:10709984};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21.4 uM for crotonyl-CoA {ECO:0000269|PubMed:10709984};
CC KM=9.0 uM for trans-2,3-pentenoyl-CoA {ECO:0000269|PubMed:10709984};
CC KM=9.1 uM for trans-2,3-hexenoyl-CoA {ECO:0000269|PubMed:10709984};
CC Vmax=2850 umol/min/mg enzyme with crotonyl-CoA as substrate
CC {ECO:0000269|PubMed:10709984};
CC Vmax=798 umol/min/mg enzyme with trans-2,3-pentenoyl-CoA as substrate
CC {ECO:0000269|PubMed:10709984};
CC Vmax=986 umol/min/mg enzyme with trans-2,3-hexenoyl-CoA as substrate
CC {ECO:0000269|PubMed:10709984};
CC Note=kcat is 728 sec(-1) with crotonyl-CoA as substrate. kcat is 204
CC sec(-1) with trans-2,3-pentenoyl-CoA as substrate. kcat is 252 sec(-
CC 1) with trans-2,3-hexenoyl-CoA as substrate.
CC {ECO:0000269|PubMed:10709984};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10709984}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF60220.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF156879; AAF60220.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP000230; ABC23759.1; -; Genomic_DNA.
DR RefSeq; WP_011390712.1; NC_007643.1.
DR RefSeq; YP_428046.1; NC_007643.1.
DR AlphaFoldDB; Q2RQ36; -.
DR SMR; Q2RQ36; -.
DR STRING; 269796.Rru_A2964; -.
DR EnsemblBacteria; ABC23759; ABC23759; Rru_A2964.
DR KEGG; rru:Rru_A2964; -.
DR PATRIC; fig|269796.9.peg.3073; -.
DR eggNOG; COG2030; Bacteria.
DR HOGENOM; CLU_094876_3_3_5; -.
DR OMA; PGPGCIY; -.
DR OrthoDB; 1563802at2; -.
DR PhylomeDB; Q2RQ36; -.
DR SABIO-RK; Q2RQ36; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042621; P:poly(3-hydroxyalkanoate) biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Fatty acid metabolism; Lipid metabolism; Lyase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10709984"
FT CHAIN 2..144
FT /note="(R)-specific enoyl-CoA hydratase"
FT /id="PRO_0000433082"
FT DOMAIN 13..128
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT CONFLICT 76
FT /note="T -> N (in Ref. 1; AAF60220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 144 AA; 15355 MW; 873B20CFAC6D960F CRC64;
MSADDLILHY FEDIKEGQSA SLAKTISESD IYLFAGLSMD TNPAHVNEDY AQTTVFKTRI
AHGMLSAGFI SAVLGTRLPG PGAIYVNQSL KFKAPVRIGD TVTATVTVTG LVPEKKFVTF
RTTCTVAGKV VIEGEATVMV PARG
