PYCR1_BURCM
ID PYCR1_BURCM Reviewed; 340 AA.
AC Q0B9S2;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Delta(1)-pyrroline-2-carboxylate reductase 1;
DE Short=Pyr2C reductase 1;
DE EC=1.5.1.49 {ECO:0000269|PubMed:24980702};
DE AltName: Full=Proline ketimine reductase 1 {ECO:0000303|PubMed:24980702};
GN OrderedLocusNames=Bamb_3547 {ECO:0000312|EMBL:ABI89101.1};
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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=9.4 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC cosubstrate) {ECO:0000269|PubMed:24980702};
CC Note=kcat is 54 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; CP000441; ABI89101.1; -; Genomic_DNA.
DR RefSeq; WP_011658570.1; NZ_CP009799.1.
DR AlphaFoldDB; Q0B9S2; -.
DR SMR; Q0B9S2; -.
DR STRING; 339670.Bamb_3547; -.
DR EnsemblBacteria; ABI89101; ABI89101; Bamb_3547.
DR GeneID; 44694187; -.
DR KEGG; bam:Bamb_3547; -.
DR PATRIC; fig|339670.21.peg.3770; -.
DR eggNOG; COG2055; Bacteria.
DR OMA; TNTEPAM; -.
DR SABIO-RK; Q0B9S2; -.
DR Proteomes; UP000000662; Chromosome 2.
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.
FT CHAIN 1..340
FT /note="Delta(1)-pyrroline-2-carboxylate reductase 1"
FT /id="PRO_0000432293"
FT ACT_SITE 50
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT ACT_SITE 51
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT ACT_SITE 191
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 123..127
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 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 181..183
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 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 232..233
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 307..313
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 340 AA; 36239 MW; B4D7E57261777F99 CRC64;
MSESLAEVVL SLDEVHALAL RVLTHNGMSA AHAQAIANVI TQGQRDECHS HGVYRLLVCV
RSLKKGKVDP QAVPTLRRLS SSIVAVDAHR GFSLLSFETG LPVLVEMAKQ HGIAAMAINH
CYHFSALWPE VEAIAAEGLV GIAMNPSHSW VAPEGGREPV FGTNPIAFAW PRPDGVPFVF
DFATSAIARG DIELHAKQGK AIPPHWAIDA DGQPTTDPKA ALQGAMRTFG GHKGSALAAM
VELLGGALIG DMTSRESMAF DEGVGATPCH GELVIAFDPK VFLGDELDAG LARGERMFAS
ITGQGARLPS QRRFDARARS IAHGVRIPKA LYDEILTLLD
