PY2CR_PSEUB
ID PY2CR_PSEUB Reviewed; 343 AA.
AC Q4U331;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Delta(1)-pyrroline-2-carboxylate/Delta(1)-piperideine-2-carboxylate reductase {ECO:0000303|PubMed:16192274};
DE Short=Pyr2C/Pip2C reductase {ECO:0000303|PubMed:16192274};
DE EC=1.5.1.21 {ECO:0000269|PubMed:16192274};
DE AltName: Full=N-methyl-L-amino acid dehydrogenase {ECO:0000303|PubMed:16192274};
DE EC=1.4.1.17 {ECO:0000269|PubMed:16192274};
GN Name=dpkA {ECO:0000303|PubMed:16192274};
GN ORFNames=NB04_21545 {ECO:0000312|EMBL:KGK93380.1};
OS Pseudomonas syringae pv. tomato.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=323;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS)
RP OF APOENZYME AND IN COMPLEXES WITH NADPH AND PYRROLE-2-CARBOXYLATE
RP INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, REACTION MECHANISM,
RP AND ACTIVE SITE.
RC STRAIN=DSM 50315;
RX PubMed=16192274; DOI=10.1074/jbc.m507399200;
RA Goto M., Muramatsu H., Mihara H., Kurihara T., Esaki N., Omi R.,
RA Miyahara I., Hirotsu K.;
RT "Crystal structures of Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-
RT carboxylate reductase belonging to a new family of NAD(P)H-dependent
RT oxidoreductases: conformational change, substrate recognition, and
RT stereochemistry of the reaction.";
RL J. Biol. Chem. 280:40875-40884(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NYS-T1;
RA Jones L.A., Saha S., Collmer A., Smart C.D., Lindeberg M.;
RT "Genome-assisted development of a diagnostic protocol for distinguishing
RT high virulence Pseudomonas syringae pv. tomato strains.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of both Delta(1)-pyrroline-2-
CC carboxylate (Pyr2C) and Delta(1)-piperideine-2-carboxylate (Pip2C) to
CC L-proline and L-pipecolate, respectively, using NADPH as the electron
CC donor. Can catalyze the reverse oxidation reactions, albeit at a much
CC lower rate. Is also able to catalyze in vitro the NADPH-dependent
CC formation of N-methylalanine from pyruvate and N-methylamine; can act
CC on other alpha-keto acids and specifically uses methylamine and not
CC ammonia for these reductive amination reactions. Can use NADH instead
CC of NADPH, although with much less efficiency.
CC {ECO:0000269|PubMed:16192274}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-pipecolate + NADP(+) = Delta(1)-piperideine-2-carboxylate +
CC H(+) + NADPH; Xref=Rhea:RHEA:12524, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61185,
CC ChEBI:CHEBI:77631; EC=1.5.1.21;
CC Evidence={ECO:0000269|PubMed:16192274};
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=1.5.1.21;
CC Evidence={ECO:0000269|PubMed:16192274};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-methyl-L-alanine + NADP(+) = H(+) + methylamine +
CC NADPH + pyruvate; Xref=Rhea:RHEA:21768, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58175, ChEBI:CHEBI:58349, ChEBI:CHEBI:59338; EC=1.4.1.17;
CC Evidence={ECO:0000269|PubMed:16192274};
CC -!- ACTIVITY REGULATION: Is inhibited by the substrate analog pyrrole-2-
CC carboxylate, and by 2-picolinate. {ECO:0000269|PubMed:16192274}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 30-45 degrees Celsius. Is stable between 0 and
CC 35 degrees Celsius after incubation of 30 minutes.
CC {ECO:0000269|PubMed:16192274};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16192274}.
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; DQ017704; AAY43734.1; -; Genomic_DNA.
DR EMBL; JRRA01000024; KGK93380.1; -; Genomic_DNA.
DR RefSeq; WP_007246364.1; NZ_SNVG01000050.1.
DR PDB; 1WTJ; X-ray; 1.55 A; A/B=1-343.
DR PDB; 2CWF; X-ray; 1.80 A; A/B=1-343.
DR PDB; 2CWH; X-ray; 1.70 A; A/B=1-343.
DR PDBsum; 1WTJ; -.
DR PDBsum; 2CWF; -.
DR PDBsum; 2CWH; -.
DR AlphaFoldDB; Q4U331; -.
DR SMR; Q4U331; -.
DR HOGENOM; CLU_040452_0_0_6; -.
DR BRENDA; 1.5.1.1; 5193.
DR BRENDA; 1.5.1.21; 5193.
DR EvolutionaryTrace; Q4U331; -.
DR GO; GO:0047125; F:delta1-piperideine-2-carboxylate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050132; F:N-methylalanine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; 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 3D-structure; NADP; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..343
FT /note="Delta(1)-pyrroline-2-carboxylate/Delta(1)-
FT piperideine-2-carboxylate reductase"
FT /id="PRO_0000432289"
FT ACT_SITE 53
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:16192274"
FT ACT_SITE 54
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:16192274"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:16192274"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16192274"
FT BINDING 126..130
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:0000269|PubMed:16192274,
FT ECO:0007744|PDB:2CWF, ECO:0007744|PDB:2CWH"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16192274"
FT BINDING 184..186
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:0000269|PubMed:16192274,
FT ECO:0007744|PDB:2CWF, ECO:0007744|PDB:2CWH"
FT BINDING 192..193
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:16192274"
FT BINDING 236..237
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:16192274,
FT ECO:0007744|PDB:2CWF, ECO:0007744|PDB:2CWH"
FT BINDING 309..315
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:0000269|PubMed:16192274,
FT ECO:0007744|PDB:2CWF, ECO:0007744|PDB:2CWH"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:1WTJ"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1WTJ"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 96..114
FT /evidence="ECO:0007829|PDB:1WTJ"
FT STRAND 115..125
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:1WTJ"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1WTJ"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1WTJ"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:1WTJ"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:1WTJ"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:1WTJ"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:1WTJ"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:1WTJ"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:1WTJ"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 291..304
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 313..325
FT /evidence="ECO:0007829|PDB:1WTJ"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1WTJ"
FT HELIX 331..340
FT /evidence="ECO:0007829|PDB:1WTJ"
SQ SEQUENCE 343 AA; 36249 MW; 7CC78CEDB2151A54 CRC64;
MSASHADQPT QTVSYPQLID LLRRIFVVHG TSPEVADVLA ENCASAQRDG SHSHGIFRIP
GYLSSLASGW VDGKAVPVVE DVGAAFVRVD ACNGFAQPAL AAARSLLIDK ARSAGVAILA
IRGSHHFAAL WPDVEPFAEQ GLVALSMVNS MTCVVPHGAR QPLFGTNPIA FGAPRAGGEP
IVFDLATSAI AHGDVQIAAR EGRLLPAGMG VDRDGLPTQE PRAILDGGAL LPFGGHKGSA
LSMMVELLAA GLTGGNFSFE FDWSKHPGAQ TPWTGQLLIV IDPDKGAGQH FAQRSEELVR
QLHGVGQERL PGDRRYLERA RSMAHGIVIA QADLERLQEL AGH
