PY2CR_PSEF5
ID PY2CR_PSEF5 Reviewed; 336 AA.
AC Q4KGT8;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Delta(1)-pyrroline-2-carboxylate reductase;
DE Short=Pyr2C reductase;
DE EC=1.5.1.49 {ECO:0000269|PubMed:24980702};
DE AltName: Full=Proline ketimine reductase {ECO:0000303|PubMed:24980702};
GN OrderedLocusNames=PFL_1416 {ECO:0000312|EMBL:AAY90701.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 Delta(1)-pyrroline-2-carboxylate
CC (Pyr2C) to L-proline, using NADPH as the electron donor. May be
CC involved in a degradation pathway that converts trans-3-hydroxy-L-
CC proline (t3LHyp) to L-proline. {ECO:0000269|PubMed:24980702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NAD(+) = 1-pyrroline-2-carboxylate + H(+) + NADH;
CC Xref=Rhea:RHEA:20321, ChEBI:CHEBI:15378, ChEBI:CHEBI:39785,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.49;
CC Evidence={ECO:0000269|PubMed:24980702};
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=1.5.1.49;
CC Evidence={ECO:0000269|PubMed:24980702};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC cosubstrate) {ECO:0000269|PubMed:24980702};
CC Note=kcat is 20 sec(-1) for Pyr2C reduction using NADPH.
CC {ECO:0000269|PubMed:24980702};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4U331}.
CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; CP000076; AAY90701.1; -; Genomic_DNA.
DR RefSeq; WP_011059758.1; NC_004129.6.
DR AlphaFoldDB; Q4KGT8; -.
DR SMR; Q4KGT8; -.
DR STRING; 220664.PFL_1416; -.
DR EnsemblBacteria; AAY90701; AAY90701; PFL_1416.
DR KEGG; pfl:PFL_1416; -.
DR PATRIC; fig|220664.5.peg.1450; -.
DR eggNOG; COG2055; Bacteria.
DR HOGENOM; CLU_040452_0_0_6; -.
DR OMA; CSDYRGH; -.
DR OrthoDB; 1374098at2; -.
DR SABIO-RK; Q4KGT8; -.
DR Proteomes; UP000008540; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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..336
FT /note="Delta(1)-pyrroline-2-carboxylate reductase"
FT /id="PRO_0000432292"
FT ACT_SITE 47
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT ACT_SITE 48
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 120..124
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 160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 178..180
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 186..187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 229..230
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 304..310
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 336 AA; 36029 MW; DA7FB9886FB53C7E CRC64;
MSEYITLSLD EVCALSYQVL TRHGLSDAHA RAIAEVITQG QRDECHSHGV YRLLGCVRSV
REGRIDPRAE PSLRHVSPGV LEVDAHYGYS LLGFHTGLPI LAEKARSQGI AAMVIKRCFH
FSALWPEVEA IADYGLVGMA MNPSHSWVAP AGGRQPVFGT NPLAFAWPRP GGQPFVFDFA
TSAIARGDIE LHARQGKPIP EHWAIDADGQ PTTDAKAALQ GAMQTFGGHK GSALAAMIEL
LAGALIGDLT SAESMAFDGG VGATPCHGEL VLAFDPRVFL GEGYEQGLER AEGLFAAIAR
QGARLPSQRR FAARARSLEH GVQIPRGLLE DIRGLL
