PYCR2_BURM1
ID PYCR2_BURM1 Reviewed; 340 AA.
AC A9ALD3;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Delta(1)-pyrroline-2-carboxylate reductase 2;
DE Short=Pyr2C reductase 2;
DE EC=1.5.1.49 {ECO:0000269|PubMed:24980702};
DE AltName: Full=Proline ketimine reductase 2 {ECO:0000303|PubMed:24980702};
GN Name=ybiC {ECO:0000312|EMBL:BAG45916.1};
GN OrderedLocusNames=Bmul_4451 {ECO:0000312|EMBL:ABX18130.1},
GN BMULJ_04059 {ECO:0000312|EMBL:BAG45916.1};
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
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=7.4 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC cosubstrate) {ECO:0000269|PubMed:24980702};
CC Note=kcat is 33 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; CP000869; ABX18130.1; -; Genomic_DNA.
DR EMBL; AP009386; BAG45916.1; -; Genomic_DNA.
DR RefSeq; WP_012217164.1; NC_010805.1.
DR AlphaFoldDB; A9ALD3; -.
DR SMR; A9ALD3; -.
DR STRING; 395019.Bmul_4451; -.
DR EnsemblBacteria; BAG45916; BAG45916; BMULJ_04059.
DR KEGG; bmj:BMULJ_04059; -.
DR KEGG; bmu:Bmul_4451; -.
DR eggNOG; COG2055; Bacteria.
DR HOGENOM; CLU_040452_0_0_4; -.
DR OMA; TNTEPAM; -.
DR SABIO-RK; A9ALD3; -.
DR Proteomes; UP000008815; 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; Reference proteome.
FT CHAIN 1..340
FT /note="Delta(1)-pyrroline-2-carboxylate reductase 2"
FT /id="PRO_0000432294"
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; 36407 MW; 96F6FCF683F6D3B4 CRC64;
MAEPIDAVVL SLDEVHALAL RVLTHHGLSD AHARAIANVI TQGQRDECHS HGVYRLLVCV
RSLRKGKVDP QAVPTLRRLS SSIVAVDAHR GFSLLSFETG LPVLVEMTKQ HGIAAMVINR
CYHFSALWPE VEAIAAEGLV GIAMNPSHSW VAPEGGKEPV FGTNPIAFAW PRPGGMPFVF
DFATSAIARG DIELHAKQGK PIPPEWAIDA QGRPTTDPQA ALQGAMRTFG GHKGSALAAM
VELLGGALIG DLTSRESMDF DEGVGATPCH GELAIAFDPK VFLGDDLDAG LARGERMFDS
IVAQGARLPS QRRFDARARS IANGVRIPRA LYDEIVALLD
