ID   PY2CR_PARDP             Reviewed;         316 AA.
AC   A1B196;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=Pden_1185 {ECO:0000312|EMBL:ABL69290.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=Pd 1222;
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 preferentially NADPH over NADH as the
CC       electron donor. Is likely involved in a degradation pathway that
CC       converts trans-3-hydroxy-L-proline (t3LHyp) to L-proline, which would
CC       allow P.denitrificans to grow on t3LHyp as a sole carbon source.
CC       {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=3.1 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC         cosubstrate) {ECO:0000269|PubMed:24980702};
CC         KM=16 mM for Delta(1)-pyrroline-2-carboxylate (using NADH as
CC         cosubstrate) {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 260 sec(-1) for Pyr2C reduction using NADPH. kcat is 81
CC         sec(-1) for Pyr2C reduction using NADH.
CC         {ECO:0000269|PubMed:24980702};
CC   -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC       family. {ECO:0000305}.
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DR   EMBL; CP000489; ABL69290.1; -; Genomic_DNA.
DR   RefSeq; WP_011747510.1; NC_008686.1.
DR   AlphaFoldDB; A1B196; -.
DR   SMR; A1B196; -.
DR   STRING; 318586.Pden_1185; -.
DR   PRIDE; A1B196; -.
DR   EnsemblBacteria; ABL69290; ABL69290; Pden_1185.
DR   KEGG; pde:Pden_1185; -.
DR   eggNOG; COG2423; Bacteria.
DR   HOGENOM; CLU_042088_1_2_5; -.
DR   OMA; AVKAFTY; -.
DR   SABIO-RK; A1B196; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1780.10; -; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003462; ODC_Mu_crystall.
DR   InterPro; IPR023401; ODC_N.
DR   PANTHER; PTHR13812; PTHR13812; 1.
DR   Pfam; PF02423; OCD_Mu_crystall; 1.
DR   PIRSF; PIRSF001439; CryM; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..316
FT                   /note="Delta(1)-pyrroline-2-carboxylate reductase"
FT                   /id="PRO_0000432297"
SQ   SEQUENCE   316 AA;  33448 MW;  EE4BC4D4906CBE04 CRC64;
     MARKSSAPQF LSYGDATGRL SWRDAVEALR QGHTLPQAQI RDVFLGPPTG TMMSRSAWIE
     GLGYGAKTFT VFDGNAARGL PTVQGAMLVF DKDDGRLQAI VDSPLVTEFK TAADSVLGAS
     LLARPDSRHL LIVGAGTVAA SLVRAYTAVL PGIERVSVWA RRPQQAQDLI EGLDGIEADL
     AAVSDLPAAV GQADIVSSAT MARQPVILGA WVRPGTHVDL IGAFKADMRE ADDALMARAA
     LFVDSRETTL GHIGELMLPI ASGAITAESV LGDLYDLVRP GARRRQSEDE ITVFKNGGGA
     HLDLMIASYI ARVMAG