ID   PY2CR_BACCZ             Reviewed;         325 AA.
AC   Q63FA5;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-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   Name=arcB {ECO:0000312|EMBL:AAU19440.1};
GN   OrderedLocusNames=BCE33L0803 {ECO:0000312|EMBL:AAU19440.1};
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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. May be involved in a degradation pathway that converts
CC       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=0.03 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC         cosubstrate) (in fact KM is inferior to 0.03 mM)
CC         {ECO:0000269|PubMed:24980702};
CC         KM=4.9 mM for Delta(1)-pyrroline-2-carboxylate (using NADH as
CC         cosubstrate) {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 5.8 sec(-1) for Pyr2C reduction using NADPH. kcat is
CC         0.87 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; CP000001; AAU19440.1; -; Genomic_DNA.
DR   RefSeq; WP_000960289.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q63FA5; -.
DR   SMR; Q63FA5; -.
DR   PRIDE; Q63FA5; -.
DR   EnsemblBacteria; AAU19440; AAU19440; BCE33L0803.
DR   KEGG; bcz:BCE33L0803; -.
DR   PATRIC; fig|288681.22.peg.4775; -.
DR   OMA; AVKAFTY; -.
DR   SABIO-RK; Q63FA5; -.
DR   Proteomes; UP000002612; 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_0000432301"
SQ   SEQUENCE   325 AA;  35267 MW;  24718C304615A951 CRC64;
     MLVISANEQR KLVNMNEVIA YAALALQEFS AERTITPIRT SLPFANEQNT ALIMPSVAEG
     LEALGLKVVT VVPENKKIGK KTINGIVMLS DFQTGEPLAL LEGSYLTMIR TGALSGVATK
     HLARHNAKTL CIIGTGEQAK GIAEAVFAVR DIEKVMLYNR TEEKAYAFAQ YIQEKFGKPA
     YVYANANEAI SEADIIVTTT NASTPVFSEK LQKGVHINAV GSFRPNMQEL PSHAIANANK
     VVVESKEAAL EETGDLQVPV REGLFEASDI HAELGQIISG EKAGRESDEE ITVFKSVGLA
     VVDIIVAKYL YEKAVERGVG ERIEF