ID   PY2CR_BACCR             Reviewed;         325 AA.
AC   Q81HB0;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=BC_0906 {ECO:0000312|EMBL:AAP07893.1};
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
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 allows
CC       B.cereus 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=0.47 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC         cosubstrate) {ECO:0000269|PubMed:24980702};
CC         KM=11 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 19
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; AE016877; AAP07893.1; -; Genomic_DNA.
DR   RefSeq; NP_830692.1; NC_004722.1.
DR   RefSeq; WP_000960316.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81HB0; -.
DR   SMR; Q81HB0; -.
DR   STRING; 226900.BC_0906; -.
DR   EnsemblBacteria; AAP07893; AAP07893; BC_0906.
DR   KEGG; bce:BC0906; -.
DR   PATRIC; fig|226900.8.peg.851; -.
DR   HOGENOM; CLU_042088_1_0_9; -.
DR   OMA; AVKAFTY; -.
DR   SABIO-RK; Q81HB0; -.
DR   Proteomes; UP000001417; 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; Reference proteome.
FT   CHAIN           1..325
FT                   /note="Delta(1)-pyrroline-2-carboxylate reductase"
FT                   /id="PRO_0000432298"
SQ   SEQUENCE   325 AA;  35336 MW;  2BB35C4624EE7727 CRC64;
     MLVISANEQR NLVNMNEVIE YAALALKEFS AERTITPIRG SLPFANEQNT ALIMPSVAEG
     LEALGVKIVT VVPQNKQIGK KTINGIVMLS DFQAGEPLAL LEGSYLTMIR TGALSGVATK
     YLARHNAKTL CIIGTGEQAK GIAEAIFAVR DIEKVILYNR TEEKAYAFAQ YIQEKFGKPA
     YVYKDPNEAV READIIVTTT NATTPVFSEI LQKGVHVNAV GSFRPSMQEL PSHAIAKANK
     VVVESKEAAL DETGDLQVPI KEGLFKANAI HAELGQIISG EKAGRENDEE ITIFKSVGLA
     VVDIIVAKYL YERALEQGVG NKIEF