UniProt: E8UB33

Database: UniProt
Entry: E8UB33_DEIML

LinkDB:  E8UB33_DEIML 
Original site:  E8UB33_DEIML

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   E8UB33_DEIML            Unreviewed;       263 AA.
AC   E8UB33;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|HAMAP-Rule:MF_01925, ECO:0000256|RuleBase:RU003903};
DE            Short=P5C reductase {ECO:0000256|HAMAP-Rule:MF_01925};
DE            Short=P5CR {ECO:0000256|HAMAP-Rule:MF_01925};
DE            EC=1.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01925, ECO:0000256|RuleBase:RU003903};
DE   AltName: Full=PCA reductase {ECO:0000256|HAMAP-Rule:MF_01925};
DE   Flags: Precursor;
GN   Name=proC {ECO:0000256|HAMAP-Rule:MF_01925};
GN   OrderedLocusNames=Deima_2639 {ECO:0000313|EMBL:ADV68272.1};
OS   Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 /
OS   LB-34).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=709986 {ECO:0000313|EMBL:ADV68272.1, ECO:0000313|Proteomes:UP000008635};
RN   [1] {ECO:0000313|EMBL:ADV68272.1, ECO:0000313|Proteomes:UP000008635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC   {ECO:0000313|Proteomes:UP000008635};
RX   PubMed=21677853; DOI=10.4056/sigs.1633949;
RA   Pukall R., Zeytun A., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA   Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA   Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brambilla E.M., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Deinococcus maricopensis type strain (LB-
RT   34).";
RL   Stand. Genomic Sci. 4:163-172(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC   {ECO:0000313|Proteomes:UP000008635};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Kyrpides N.,
RA   Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A.,
RA   Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Pukall R., Gehrich-Schroeter G.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Deinococcus maricopensis DSM 21211.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC       L-proline. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01925,
CC         ECO:0000256|RuleBase:RU003903};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC       from L-glutamate 5-semialdehyde: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01925, ECO:0000256|RuleBase:RU003903}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525, ECO:0000256|HAMAP-Rule:MF_01925,
CC       ECO:0000256|RuleBase:RU003903}.
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DR   EMBL; CP002454; ADV68272.1; -; Genomic_DNA.
DR   RefSeq; WP_013557776.1; NC_014958.1.
DR   AlphaFoldDB; E8UB33; -.
DR   STRING; 709986.Deima_2639; -.
DR   KEGG; dmr:Deima_2639; -.
DR   eggNOG; COG0345; Bacteria.
DR   HOGENOM; CLU_042344_4_1_0; -.
DR   OrthoDB; 9805754at2; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000008635; 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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.10.3730.10; ProC C-terminal domain-like; 1.
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   NCBIfam; TIGR00112; proC; 1.
DR   PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR   PANTHER; PTHR11645:SF0; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01925};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008635}.
FT   DOMAIN          2..92
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          155..258
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
SQ   SEQUENCE   263 AA;  27378 MW;  6F1C2324CAAC7E2F CRC64;
     MKLAIVGVGK LGLALLEGLV RRGVLAPEEI GLLDANTVRA AEIAAQFGAR TLSESEVSRA
     ARVVVSVQPR VFPQLIEWLA QPNTGYISTM AGVSVTTLTR RLGTKRVVRV MPNLAATIGR
     AQTAITGPKE ASDAGDLEFA RMLFSAVGDT YELPEHLFNA FTGMSASGPA YAAIVAEALA
     DGGVRMGLPR PLAQELAAKL LASSGELLLE RAHPGMLKDE VASPGGTTIA GVEALERAGV
     RGGLIDAVVA ATRRATELGK DQE
//

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