P5CR_VIBAL
ID P5CR_VIBAL Reviewed; 272 AA.
AC P52053;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000255|HAMAP-Rule:MF_01925};
DE Short=P5C reductase {ECO:0000255|HAMAP-Rule:MF_01925};
DE Short=P5CR {ECO:0000255|HAMAP-Rule:MF_01925};
DE EC=1.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01925};
DE AltName: Full=PCA reductase {ECO:0000255|HAMAP-Rule:MF_01925};
GN Name=proC {ECO:0000255|HAMAP-Rule:MF_01925};
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=138-2;
RX PubMed=8982386; DOI=10.1016/s0005-2728(96)00097-7;
RA Nakamura T., Katoh Y., Shimizu Y., Matsuba Y., Unemoto T.;
RT "Cloning and sequencing of novel genes from Vibrio alginolyticus that
RT support the growth of K+ uptake-deficient mutant of Escherichia coli.";
RL Biochim. Biophys. Acta 1277:201-208(1996).
CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC L-proline. {ECO:0000255|HAMAP-Rule:MF_01925}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01925};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01925};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01925}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01925}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09063.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D50472; BAA09063.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P52053; -.
DR SMR; P52053; -.
DR STRING; 663.BAU10_12660; -.
DR eggNOG; COG0345; Bacteria.
DR UniPathway; UPA00098; UER00361.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01925; P5C_reductase; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR InterPro; IPR029036; P5CR_dimer.
DR InterPro; IPR000304; Pyrroline-COOH_reductase.
DR PANTHER; PTHR11645; PTHR11645; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00112; proC; 1.
DR PROSITE; PS00521; P5CR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Proline biosynthesis.
FT CHAIN 1..272
FT /note="Pyrroline-5-carboxylate reductase"
FT /id="PRO_0000187311"
SQ SEQUENCE 272 AA; 29026 MW; E4DFB9AC718C4AA9 CRC64;
MEHKKIAFIG AGNMVRAIVS GLVANGYPAQ NITATAPSEA RRLPLEQDFG IRTTSDNIQA
ATEADVVVLS VKPQMMADVC KPLQAIDFTN KLVISIAAGI NCSRLDDMLA TKLNLVRVMP
NTPSQLGLGM SGLFAPIHVT EHDKAFAAEL MEAVGKVCWV EQESGINNVI AAAGSAPAYF
FLFMEAMQAE AIAQGFDKES ARLLVQQAAL GAASMVVSNP ETELSTLREN VTSKGGTTAE
ALRTFNEHQL SDIVAKAMQA AVARAEEMEK LF
