ID   PY2CR_BACHK             Reviewed;         325 AA.
AC   Q6HMS8;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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:AAT59164.1};
GN   OrderedLocusNames=BT9727_0800 {ECO:0000312|EMBL:AAT59164.1};
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
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. 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=3.4 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC         cosubstrate) {ECO:0000269|PubMed:24980702};
CC         KM=18 mM for Delta(1)-pyrroline-2-carboxylate (using NADH as
CC         cosubstrate) {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 11 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; AE017355; AAT59164.1; -; Genomic_DNA.
DR   RefSeq; WP_000960294.1; NC_005957.1.
DR   RefSeq; YP_035143.1; NC_005957.1.
DR   AlphaFoldDB; Q6HMS8; -.
DR   SMR; Q6HMS8; -.
DR   EnsemblBacteria; AAT59164; AAT59164; BT9727_0800.
DR   KEGG; btk:BT9727_0800; -.
DR   PATRIC; fig|281309.8.peg.836; -.
DR   HOGENOM; CLU_042088_1_0_9; -.
DR   OMA; AVKAFTY; -.
DR   SABIO-RK; Q6HMS8; -.
DR   Proteomes; UP000001301; 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_0000432300"
SQ   SEQUENCE   325 AA;  34982 MW;  8413A725F92EB951 CRC64;
     MLVISANEQR NLVNMNEVIA YAALALKEFS AERTITPIRG SLPFANEKNT ALIMPSVAEG
     LEALGLKVVT VVPENKKIGK KTINGIVMLS DFQTGEPLAL LEGSYLTMIR TGALSGVATK
     HLARHNAKTL CIIGTGEQAK GIAEAVFAVR DIEKVILYNR TEEKAYAFSQ YIQEKFGKPA
     YVHTNANEAI SEADIIVTTT NASTPVFSEK LQKGVHVNAV GSFKPSMQEL PSHAIVGANK
     VVVESKEAAL DETGDLQVPI KEGLFKANAI HAELGQIISG EKAGRENDEE ITVFKSVGLA
     VVDIIVAKYL YEKAVESGVG NKIEF