ID   PYCR1_BURM1             Reviewed;         310 AA.
AC   A9AKH1;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Delta(1)-pyrroline-2-carboxylate reductase 1;
DE            Short=Pyr2C reductase 1;
DE            EC=1.5.1.49 {ECO:0000269|PubMed:24980702};
DE   AltName: Full=Proline ketimine reductase 1 {ECO:0000303|PubMed:24980702};
GN   Name=ocd {ECO:0000312|EMBL:BAG46100.1};
GN   OrderedLocusNames=Bmul_4263 {ECO:0000312|EMBL:ABX17944.1},
GN   BMULJ_04243 {ECO:0000312|EMBL:BAG46100.1};
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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 NADPH as the electron donor. May be
CC       involved in a degradation pathway that converts trans-3-hydroxy-L-
CC       proline (t3LHyp) to L-proline. {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=4 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC         cosubstrate) {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 25 sec(-1) for Pyr2C reduction using NADPH.
CC         {ECO:0000269|PubMed:24980702};
CC   -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000869; ABX17944.1; -; Genomic_DNA.
DR   EMBL; AP009386; BAG46100.1; -; Genomic_DNA.
DR   RefSeq; WP_012217015.1; NC_010805.1.
DR   AlphaFoldDB; A9AKH1; -.
DR   SMR; A9AKH1; -.
DR   STRING; 395019.Bmul_4263; -.
DR   EnsemblBacteria; BAG46100; BAG46100; BMULJ_04243.
DR   KEGG; bmj:BMULJ_04243; -.
DR   KEGG; bmu:Bmul_4263; -.
DR   eggNOG; COG2423; Bacteria.
DR   HOGENOM; CLU_042088_1_2_4; -.
DR   OMA; QARWQTR; -.
DR   SABIO-RK; A9AKH1; -.
DR   Proteomes; UP000008815; Chromosome 2.
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   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..310
FT                   /note="Delta(1)-pyrroline-2-carboxylate reductase 1"
FT                   /id="PRO_0000432303"
SQ   SEQUENCE   310 AA;  32236 MW;  91B4263B3AB27E59 CRC64;
     MTALSRTPVF DAADTAALLD YPALLATLAR TVADYAAGEI VSPERLVVPL QAGGVMLSMP
     SSAHDLAIHK LVNVCPGNAA RGLPTILGQV IACDATTGEM RFVLDGPTVT GRRTAAVTAL
     GVQALHGTPR EILLIGTGKQ AANHAEAFTA LFPDARLHVR GSRAASAAEF CAAHRAHAPQ
     LMPLDGDAIP DAIDVVVTLT TSRTPVYRDA AREGRLVVGV GAFTADAAEI AADTVRRSRL
     VVDDPAGARH EAGDLIVANV DWQQVASLAD VLNGTFARGG PMLFKTVGCA AWDLAACRTA
     RDALAAREQR