PY2CR_AGRFC
ID PY2CR_AGRFC Reviewed; 345 AA.
AC Q7CVK1;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 81.
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=Atu4676 {ECO:0000312|EMBL:AAK88773.2};
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=C58 / ATCC 33970;
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. Is likely
CC involved in a degradation pathway that converts trans-3-hydroxy-L-
CC proline (t3LHyp) to L-proline, which would allow A.tumefaciens to grow
CC on t3LHyp as a sole carbon source. {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=0.33 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH as
CC cosubstrate) {ECO:0000269|PubMed:24980702};
CC Note=kcat is 32 sec(-1) for Pyr2C reduction using NADPH.
CC {ECO:0000269|PubMed:24980702};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4U331}.
CC -!- INDUCTION: Is up-regulated when the bacterium is grown on t4LHyp or
CC t3LHyp as sole carbon source. {ECO:0000269|PubMed:24980702}.
CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC {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; AE007870; AAK88773.2; -; Genomic_DNA.
DR RefSeq; NP_355988.2; NC_003063.2.
DR RefSeq; WP_010974066.1; NC_003063.2.
DR AlphaFoldDB; Q7CVK1; -.
DR SMR; Q7CVK1; -.
DR STRING; 176299.Atu4676; -.
DR EnsemblBacteria; AAK88773; AAK88773; Atu4676.
DR KEGG; atu:Atu4676; -.
DR PATRIC; fig|176299.10.peg.4481; -.
DR eggNOG; COG2055; Bacteria.
DR HOGENOM; CLU_040452_0_0_5; -.
DR OMA; ISHMAPH; -.
DR PhylomeDB; Q7CVK1; -.
DR BioCyc; AGRO:ATU4676-MON; -.
DR SABIO-RK; Q7CVK1; -.
DR Proteomes; UP000000813; Chromosome linear.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1530.10; -; 1.
DR Gene3D; 3.30.1370.60; -; 1.
DR InterPro; IPR043144; Mal/L-sulf/L-lact_DH-like_ah.
DR InterPro; IPR043143; Mal/L-sulf/L-lact_DH-like_NADP.
DR InterPro; IPR036111; Mal/L-sulfo/L-lacto_DH-like_sf.
DR InterPro; IPR003767; Malate/L-lactate_DH-like.
DR PANTHER; PTHR11091; PTHR11091; 1.
DR Pfam; PF02615; Ldh_2; 1.
DR SUPFAM; SSF89733; SSF89733; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..345
FT /note="Delta(1)-pyrroline-2-carboxylate reductase"
FT /id="PRO_0000432291"
FT ACT_SITE 47
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT ACT_SITE 48
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT ACT_SITE 189
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 121..125
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 179..181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 230..231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 305..311
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
SQ SEQUENCE 345 AA; 36189 MW; DFB79EC52F995C33 CRC64;
MSDTTTLTIE ALFQRVESIF LRAGLNAVQS GALARVITAG ERDACKSHGI YRIEGALRTV
KAAKVKPDAI PEVAEDDGTA IVKVNAMGGF ANPAFELGLP ALAERAKRLG LAALVINDCT
HFSALWPEVE GLTSNGLAGL VMCPSYSTVA PTGGTKPLLG TNPFAFGWPR KDTSPYVFDF
ATSVAARGEI ELHRRARKSL PEGWAVDADG NPTTDPEAAL AGAMLPFGGH KGSAIGTMIE
LLAGIMIGDL TSPEVLDYLG TTTLAPFHGE LIVAFSPEAF AKGRPGDPFQ RAEVLFEAII
GQGARLPSGR RFAARAKSES EGITLTAAEM AGLDRLLEKG LDAVS
