ID   PY2CR_BACC1             Reviewed;         325 AA.
AC   Q73CR9;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=BCE_0995 {ECO:0000312|EMBL:AAS39926.1};
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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 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.
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=1.1 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC         cosubstrate) {ECO:0000269|PubMed:24980702};
CC         KM=7.6 mM for Delta(1)-pyrroline-2-carboxylate (using NADH as
CC         cosubstrate) {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 15 sec(-1) for Pyr2C reduction using NADPH. kcat is 2.1
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; AE017194; AAS39926.1; -; Genomic_DNA.
DR   RefSeq; WP_000960303.1; NC_003909.8.
DR   AlphaFoldDB; Q73CR9; -.
DR   SMR; Q73CR9; -.
DR   EnsemblBacteria; AAS39926; AAS39926; BCE_0995.
DR   GeneID; 59158716; -.
DR   KEGG; bca:BCE_0995; -.
DR   HOGENOM; CLU_042088_1_0_9; -.
DR   OMA; AVKAFTY; -.
DR   SABIO-RK; Q73CR9; -.
DR   Proteomes; UP000002527; Chromosome.
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.
FT   CHAIN           1..325
FT                   /note="Delta(1)-pyrroline-2-carboxylate reductase"
FT                   /id="PRO_0000432299"
SQ   SEQUENCE   325 AA;  35315 MW;  9DBA0D66F5E1C78B CRC64;
     MLVISANEQR NLVNMNEVIE YAALALKEFS AERTITPIRD SLPFANEQNT ALIMPSVAEG
     LEALGLKVVT VVPENKKIGK KTINGIVMLS DFQTGEPLAL LEGSYLTMIR TGALSGVATK
     HLARHNAKTL CIIGTGEQAK GIAEAVFAVR DIEKVILYNR TEEKAYAFSQ YIQEKFNKPA
     YVYTSANEAI SEADIIATTT NASTPVFSKK LQKGVHVNAV GSFRPSMQEL PSHAIANATK
     VVVESKEAAL EETGDLQVPI QEGLFKSSDI HAELGQIISG EKAGRESDEE VTVFKSVGLA
     VVDIIVAKYL YERAVERGVG ERIEF