P5CR_MYCLE
ID P5CR_MYCLE Reviewed; 294 AA.
AC P46725;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 123.
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}; OrderedLocusNames=ML2430;
GN ORFNames=B2168_C2_211;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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}.
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DR EMBL; U00018; AAA17233.1; -; Genomic_DNA.
DR EMBL; AL583925; CAC31947.1; -; Genomic_DNA.
DR PIR; S72897; S72897.
DR RefSeq; NP_302575.1; NC_002677.1.
DR RefSeq; WP_010908894.1; NC_002677.1.
DR AlphaFoldDB; P46725; -.
DR SMR; P46725; -.
DR STRING; 272631.ML2430; -.
DR EnsemblBacteria; CAC31947; CAC31947; CAC31947.
DR KEGG; mle:ML2430; -.
DR PATRIC; fig|272631.5.peg.4669; -.
DR Leproma; ML2430; -.
DR eggNOG; COG0345; Bacteria.
DR HOGENOM; CLU_042344_0_0_11; -.
DR OMA; VVRVMTN; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000000806; Chromosome.
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; Reference proteome.
FT CHAIN 1..294
FT /note="Pyrroline-5-carboxylate reductase"
FT /id="PRO_0000187293"
SQ SEQUENCE 294 AA; 30237 MW; EA8606C9CBBB6D9D CRC64;
MLSSMARIAI IGGGSIGEAL LSGLLRAGRQ VKDLVVAERM PDRARYLADT YSVLVTSVTD
AVENAMFVVV AVKPTDVESV MGDLVQAAAV ANDSAEQVLV TVAAGVTITY LESKLPAGTP
VVRAMPNAAA LVGAGVTVLA KGRFVTGQQF EDVLAMFDAV GGVLTVPESQ MDAVTAVSGS
GPAYFFLLVE ALVDAGVAVG LTRQVATELA AQTMAGSAAM LLERMDQDRH SAEVAPLGAQ
VDVPAAQLRA TITSPGGTTA AALRELERGG LRMVVDAAVQ AAKIRSEQLR ITSE
