PY2CR_AZOBR
ID PY2CR_AZOBR Reviewed; 311 AA.
AC V5YW53;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Delta(1)-pyrroline-2-carboxylate/Delta(1)-piperideine-2-carboxylate reductase {ECO:0000303|PubMed:24649405};
DE Short=Pyr2C/Pip2C reductase {ECO:0000303|PubMed:24649405};
DE EC=1.5.1.1 {ECO:0000269|PubMed:24649405};
GN Name=lhpI {ECO:0000303|PubMed:24649405};
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=24649405; DOI=10.1016/j.fob.2014.02.010;
RA Watanabe S., Tanimoto Y., Yamauchi S., Tozawa Y., Sawayama S., Watanabe Y.;
RT "Identification and characterization of trans-3-hydroxy-L-proline
RT dehydratase and Delta(1)-pyrroline-2-carboxylate reductase involved in
RT trans-3-hydroxy-L-proline metabolism of bacteria.";
RL FEBS Open Bio 4:240-250(2014).
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 or NADH as the
CC electron donor. Can also catalyze the reverse oxidation reactions,
CC albeit at a much lower rate. Together with LhpH, is involved in a
CC trans-3-hydroxy-L-proline (t3LHyp) degradation pathway to L-proline,
CC which allows A.brasilense to grow on t3LHyp as a sole carbon source.
CC Also appears to be involved in D-proline and D-lysine metabolism. Does
CC not show ornithine cyclodeaminase (OCD) activity.
CC {ECO:0000269|PubMed:24649405}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-pipecolate + NAD(+) = Delta(1)-piperideine-2-carboxylate +
CC H(+) + NADH; Xref=Rhea:RHEA:30807, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:61185,
CC ChEBI:CHEBI:77631; EC=1.5.1.1;
CC Evidence={ECO:0000269|PubMed:24649405};
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=1.5.1.1;
CC Evidence={ECO:0000269|PubMed:24649405};
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=1.5.1.1;
CC Evidence={ECO:0000269|PubMed:24649405};
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=1.5.1.1;
CC Evidence={ECO:0000269|PubMed:24649405};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.628 mM for Delta(1)-pyrroline-2-carboxylate (using NADPH, at pH
CC 6.5) {ECO:0000269|PubMed:24649405};
CC KM=0.837 mM for Delta(1)-pyrroline-2-carboxylate (using NADH, at pH
CC 6.5) {ECO:0000269|PubMed:24649405};
CC KM=0.474 mM for Delta(1)-piperideine-2-carboxylate (using NADPH, at
CC pH 6.5) {ECO:0000269|PubMed:24649405};
CC KM=0.600 mM for Delta(1)-piperideine-2-carboxylate (using NADH, at pH
CC 6.5) {ECO:0000269|PubMed:24649405};
CC KM=0.491 mM for Delta(1)-pyrroline-(4S)-hydroxy-2-carboxylate (using
CC NADPH, at pH 6.5) {ECO:0000269|PubMed:24649405};
CC KM=3.63 mM for L-proline (using NADP(+), at pH 10.5)
CC {ECO:0000269|PubMed:24649405};
CC KM=3.99 mM for L-proline (using NAD(+), at pH 10.5)
CC {ECO:0000269|PubMed:24649405};
CC KM=6.54 mM for L-pipecolate (using NADP(+), at pH 10.5)
CC {ECO:0000269|PubMed:24649405};
CC KM=14.8 mM for L-pipecolate (using NAD(+), at pH 10.5)
CC {ECO:0000269|PubMed:24649405};
CC Note=kcat is 31400 min(-1) for Pyr2C reduction using NADPH. kcat is
CC 36900 min(-1) for Pyr2C reduction using NADH. kcat is 9950 min(-1)
CC for Pip2C reduction using NADPH. kcat is 9690 min(-1) for Pip2C
CC reduction using NADH. kcat is 621 min(-1) for Delta(1)-pyrroline-
CC (4S)-hydroxy-2-carboxylate (Pyr4SH2C) reduction using NADPH. kcat is
CC 235 min(-1) for L-proline oxidation using NADP(+). kcat is 254 min(-
CC 1) for L-proline oxidation using NAD(+). kcat is 150 min(-1) for L-
CC pipecolate oxidation using NADP(+). kcat is 222 min(-1) for L-
CC pipecolate oxidation using NAD(+). {ECO:0000269|PubMed:24649405};
CC pH dependence:
CC Optimum pH is 6.5 for Pyr2C reduction and 10.5 for L-proline
CC oxidation. {ECO:0000269|PubMed:24649405};
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000269|PubMed:24649405}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24649405}.
CC -!- INDUCTION: Induced by trans-3-hydroxy-L-proline (T3LHyp), D-proline and
CC D-lysine, but not by trans-4-hydroxy-L-proline (T4LHyp) and by cis-4-
CC hydroxy-D-proline (C4DHyp). {ECO:0000269|PubMed:24649405}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene leads to loss of growth
CC on T3LHyp, D-proline and D-lysine as a sole carbon source, indicating
CC that this gene has dual metabolic functions as a reductase for Pyr2C
CC and Pip2C in these pathways. On the other hand, there is no difference
CC in growth on other carbon sources, including T4LHyp, between the wild-
CC type and mutant strains.
CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC family. {ECO:0000305|PubMed:24649405}.
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DR EMBL; AB894495; BAO21622.1; -; Genomic_DNA.
DR AlphaFoldDB; V5YW53; -.
DR SMR; V5YW53; -.
DR BioCyc; MetaCyc:MON-18703; -.
DR BRENDA; 1.5.1.1; 611.
DR SABIO-RK; V5YW53; -.
DR GO; GO:0047125; F:delta1-piperideine-2-carboxylate reductase activity; IEA:RHEA.
DR GO; GO:0050241; F:pyrroline-2-carboxylate reductase activity; IEA:UniProtKB-EC.
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..311
FT /note="Delta(1)-pyrroline-2-carboxylate/Delta(1)-
FT piperideine-2-carboxylate reductase"
FT /id="PRO_0000432295"
SQ SEQUENCE 311 AA; 31831 MW; 2059EC3659AA6136 CRC64;
MTALSPIPVF DAADTAALLA YPALLATLGQ AVADYAAGEI VSPERLVVPL QAGGVMLSMP
SSARDLATHK LVNVCPGNGA RGLPTILGQV TAYDASTGEM RFALDGPTVT GRRTAAVTAL
GIQALHGAAP RDILLIGTGK QAANHAEALA AIFPEARLHV RGTSADSAAA FCAAHRAQAP
RLVPLDGDAI PDAIDVVVTL TTSRTPVYRE AAREGRLVVG VGAFTADAAE IDANTVRASR
LVVDDPAGAR HEAGDLIVAQ VDWQHVASLA DVLGGTFDRS GPLLFKSVGC AAWDLAACRT
ARDALAARRA G
