PY2CR_PSEAE
ID PY2CR_PSEAE Reviewed; 334 AA.
AC Q9I492;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Delta(1)-pyrroline-2-carboxylate/Delta(1)-piperideine-2-carboxylate reductase {ECO:0000303|PubMed:24649405};
DE Short=Pyr2C/Pip2C reductase {ECO:0000303|PubMed:24649405};
DE EC=1.5.1.21 {ECO:0000269|PubMed:24649405, ECO:0000269|PubMed:24980702};
DE AltName: Full=Delta(1)-pyrroline-(4S)-hydroxy-2-carboxylate reductase {ECO:0000303|PubMed:24649405};
DE Short=Pyr4SH2C reductase {ECO:0000303|PubMed:24649405};
DE EC=1.5.1.- {ECO:0000269|PubMed:24649405};
DE AltName: Full=Proline ketimine reductase {ECO:0000303|PubMed:24980702};
GN Name=lhpD {ECO:0000303|PubMed:24649405}; OrderedLocusNames=PA1252;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=24649405; DOI=10.1016/j.fob.2014.02.010;
RA Watanabe S., Tanimoto Y., Yamauchi S., Tozawa Y., Sawayama S., Watanabe Y.;
RT "Identification and characterization of trans-3-hydroxy-L-proline
RT dehydratase and Delta(1)-pyrroline-2-carboxylate reductase involved in
RT trans-3-hydroxy-L-proline metabolism of bacteria.";
RL FEBS Open Bio 4:240-250(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=24980702; DOI=10.7554/elife.03275;
RA Zhao S., Sakai A., Zhang X., Vetting M.W., Kumar R., Hillerich B.,
RA San Francisco B., Solbiati J., Steves A., Brown S., Akiva E., Barber A.,
RA Seidel R.D., Babbitt P.C., Almo S.C., Gerlt J.A., Jacobson M.P.;
RT "Prediction and characterization of enzymatic activities guided by sequence
RT similarity and genome neighborhood networks.";
RL Elife 3:E03275-E03275(2014).
CC -!- FUNCTION: Catalyzes the reduction of both Delta(1)-pyrroline-2-
CC carboxylate (Pyr2C) and Delta(1)-piperideine-2-carboxylate (Pip2C) to
CC L-proline and L-pipecolate, respectively, using NADPH as the electron
CC donor. Cannot use NADH instead of NADPH. Is likely involved in a
CC degradation pathway that converts trans-3-hydroxy-L-proline (t3LHyp) to
CC L-proline, which would allow P.aeruginosa to grow on t3LHyp as a sole
CC carbon source. Can also catalyze the reverse oxidation reactions,
CC albeit at a much lower rate. Is also able to use Delta(1)-pyrroline-
CC (4S)-hydroxy-2-carboxylate (Pyr4SH2C) and cis-4-hydroxy-L-proline
CC (c4LHyp) as substrates, and might be involved in the metabolism of
CC c4LHyp, a compound which is generated by the hydroxylation of free L-
CC proline in bacteria. {ECO:0000269|PubMed:24649405,
CC ECO:0000269|PubMed:24980702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-pipecolate + NADP(+) = Delta(1)-piperideine-2-carboxylate +
CC H(+) + NADPH; Xref=Rhea:RHEA:12524, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61185,
CC ChEBI:CHEBI:77631; EC=1.5.1.21;
CC Evidence={ECO:0000269|PubMed:24649405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NADP(+) = 1-pyrroline-2-carboxylate + H(+) +
CC NADPH; Xref=Rhea:RHEA:20317, ChEBI:CHEBI:15378, ChEBI:CHEBI:39785,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.21;
CC Evidence={ECO:0000269|PubMed:24649405, ECO:0000269|PubMed:24980702};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cis-4-hydroxy-L-proline + NADP(+) = Delta(1)-pyrroline-(4S)-
CC hydroxy-2-carboxylate + 2 H(+) + NADPH; Xref=Rhea:RHEA:47688,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:63727, ChEBI:CHEBI:87834;
CC Evidence={ECO:0000269|PubMed:24649405};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.447 mM for Delta(1)-pyrroline-2-carboxylate (at pH 7.0)
CC {ECO:0000269|PubMed:24649405};
CC KM=1.57 mM for Delta(1)-piperideine-2-carboxylate (at pH 7.0)
CC {ECO:0000269|PubMed:24649405};
CC KM=0.835 mM for Delta(1)-pyrroline-(4S)-hydroxy-2-carboxylate (at pH
CC 7.0) {ECO:0000269|PubMed:24649405};
CC KM=18.5 mM for L-proline (at pH 10.0) {ECO:0000269|PubMed:24649405};
CC KM=34.8 mM for L-pipecolate (at pH 10.0)
CC {ECO:0000269|PubMed:24649405};
CC KM=132 mM for trans-3-hydroxy-L-proline (at pH 10.0)
CC {ECO:0000269|PubMed:24649405};
CC KM=0.41 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC cosubstrate) {ECO:0000269|PubMed:24980702};
CC Note=kcat is 2500 min(-1) for Pyr2C reduction. kcat is 2120 min(-1)
CC for Pip2C reduction. kcat is 868 min(-1) for Pyr4SH2C reduction. kcat
CC is 205 min(-1) for L-proline oxidation. kcat is 135 min(-1) for L-
CC pipecolate oxidation. kcat is 272 min(-1) for t3LHyp oxidation.
CC {ECO:0000269|PubMed:24649405};
CC pH dependence:
CC Optimum pH is 7.0 for Pyr2C reduction and 10.0 for L-proline
CC oxidation. {ECO:0000269|PubMed:24649405};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24649405}.
CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG04641.1; -; Genomic_DNA.
DR PIR; B83488; B83488.
DR RefSeq; NP_249943.1; NC_002516.2.
DR RefSeq; WP_003082545.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I492; -.
DR SMR; Q9I492; -.
DR STRING; 287.DR97_685; -.
DR PaxDb; Q9I492; -.
DR PRIDE; Q9I492; -.
DR DNASU; 881290; -.
DR EnsemblBacteria; AAG04641; AAG04641; PA1252.
DR GeneID; 881290; -.
DR KEGG; pae:PA1252; -.
DR PATRIC; fig|208964.12.peg.1300; -.
DR PseudoCAP; PA1252; -.
DR HOGENOM; CLU_040452_0_0_6; -.
DR InParanoid; Q9I492; -.
DR OMA; TNTEPAM; -.
DR PhylomeDB; Q9I492; -.
DR BioCyc; PAER208964:G1FZ6-1277-MON; -.
DR BRENDA; 1.5.1.21; 5087.
DR SABIO-RK; Q9I492; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0047125; F:delta1-piperideine-2-carboxylate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019470; P:4-hydroxyproline catabolic process; IDA:PseudoCAP.
DR Gene3D; 1.10.1530.10; -; 1.
DR Gene3D; 3.30.1370.60; -; 1.
DR InterPro; IPR043144; Mal/L-sulf/L-lact_DH-like_ah.
DR InterPro; IPR043143; Mal/L-sulf/L-lact_DH-like_NADP.
DR InterPro; IPR036111; Mal/L-sulfo/L-lacto_DH-like_sf.
DR InterPro; IPR003767; Malate/L-lactate_DH-like.
DR PANTHER; PTHR11091; PTHR11091; 1.
DR Pfam; PF02615; Ldh_2; 1.
DR SUPFAM; SSF89733; SSF89733; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="Delta(1)-pyrroline-2-carboxylate/Delta(1)-
FT piperideine-2-carboxylate reductase"
FT /id="PRO_0000083843"
FT ACT_SITE 44
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT ACT_SITE 45
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT ACT_SITE 185
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 117..121
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 175..177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 226..227
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 301..307
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
SQ SEQUENCE 334 AA; 35684 MW; EF9A6AB407515A7E CRC64;
MIRMTLDEVR ELAVRILRRH AFSEAHVQAV ADTLVAGERD ECASHGIWRL LGCIATLKAG
KVSADAEPEL HDIAPGLLRV DAHGGFSQCA FRLGLPHLLE KARSQGIAAM AVNRCVHFSA
LWVEVEALTE AGLVALATTP SHAWVAPAGG RKPIFGTNPI AFGWPRPDGP PFVFDFATSA
VARGEIQLHE RAGKPIPLGW GVDEQGEPTT DASAALRGAM LTFGGHKGSA LAAMVELLAG
PLIGDLTSAE SLAYDEGSRS SPYGGELLIA IDPRRMLGAS AEEHLARAET LFEGIVEQGA
RLPSQRRFEA RERSARDGVT IPEALHRELL ALLE
