PY2CR_STAND
ID PY2CR_STAND Reviewed; 341 AA.
AC D7A0Y0;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Delta(1)-pyrroline-2-carboxylate reductase {ECO:0000303|PubMed:25608448};
DE Short=Pyr2C reductase {ECO:0000303|PubMed:25608448};
DE EC=1.5.1.49 {ECO:0000269|PubMed:25608448};
GN OrderedLocusNames=Snov_0154 {ECO:0000312|EMBL:ADH87490.1};
OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS 12100 / NBRC 12443 / NCIMB 10456).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Starkeya.
OX NCBI_TaxID=639283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443
RC / NCIMB 10456;
RX PubMed=23450099; DOI=10.4056/sigs.3006378;
RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA Ivanova N., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the facultatively chemolithoautotrophic and
RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT 8093(T)).";
RL Stand. Genomic Sci. 7:44-58(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443
RC / NCIMB 10456;
RX PubMed=25608448; DOI=10.1021/ja5103986;
RA Zhang X., Kumar R., Vetting M.W., Zhao S., Jacobson M.P., Almo S.C.,
RA Gerlt J.A.;
RT "A unique cis-3-hydroxy-L-proline dehydratase in the enolase superfamily.";
RL J. Am. Chem. Soc. 137:1388-1391(2015).
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 cis- and trans-3-
CC hydroxy-L-proline (c3LHyp and t3LHyp) to L-proline, which would allow
CC S.novella to grow on c3LHyp or t3LHyp as a sole carbon source.
CC {ECO:0000269|PubMed:25608448}.
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:25608448};
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:25608448};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.8 mM for 1-pyrroline-2-carboxylate
CC {ECO:0000269|PubMed:25608448};
CC Note=kcat is 26 sec(-1) for Pyr2C reduction using NADPH.
CC {ECO:0000269|PubMed:25608448};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4U331}.
CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; CP002026; ADH87490.1; -; Genomic_DNA.
DR RefSeq; WP_013164995.1; NC_014217.1.
DR AlphaFoldDB; D7A0Y0; -.
DR SMR; D7A0Y0; -.
DR STRING; 639283.Snov_0154; -.
DR EnsemblBacteria; ADH87490; ADH87490; Snov_0154.
DR KEGG; sno:Snov_0154; -.
DR eggNOG; COG2055; Bacteria.
DR HOGENOM; CLU_040452_0_0_5; -.
DR OMA; IGWVTAK; -.
DR OrthoDB; 1374098at2; -.
DR Proteomes; UP000006633; Chromosome.
DR GO; GO:0050241; F:pyrroline-2-carboxylate reductase activity; IDA:UniProtKB.
DR GO; GO:0006560; P:proline metabolic process; IDA:UniProtKB.
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..341
FT /note="Delta(1)-pyrroline-2-carboxylate reductase"
FT /id="PRO_0000433400"
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 188
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 120..124
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 160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 178..180
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 186..187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4U331"
FT BINDING 229..230
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 341 AA; 35221 MW; E145E66A60A73D15 CRC64;
MDEPVRLSLA EVHVLCRDTL VAAGLGEEHA QAIARSITRA EADECHSHGL YRLIGYVASV
RSGKAERHAL PALARATPAV LRVDAKHGFA PLAVETGVPA LIAAAKEIGI AALAIHDCYH
FSALWADIEP AVEAGLAAWC FTVGQCCVAP AGGTTPLLGT NPFAFGWPGP SGRPFIFDFA
TSAAARGEIE LKRRGGEKIP PGWAVGPDGA PTTDPAAALA GALLPFGGHK GSALSMMVEL
IAGPLIGDLT SRQSKAVENG DGGPPLGGEL FIAIDPAVFG TGNLSSRLAD ADELFALAKA
QPGVRLPSER RYQARERSRT NGIAVPAALF AELQALGPRG S
