(data stored in ACNUC7421 zone)

SWISSPROT: Q4ZZ76_PSEU2

ID   Q4ZZ76_PSEU2            Unreviewed;       272 AA.
AC   Q4ZZ76;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 103.
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};
GN   Name=proC {ECO:0000256|HAMAP-Rule:MF_01925};
GN   OrderedLocusNames=Psyr_0476 {ECO:0000313|EMBL:AAY35546.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35546.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35546.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35546.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate
CC       (PCA) to 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,
CC         ChEBI:CHEBI:15893, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:60039; EC=1.5.1.2; Evidence={ECO:0000256|HAMAP-
CC         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,
CC         ChEBI:CHEBI:15893, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:60039; EC=1.5.1.2; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01925, ECO:0000256|RuleBase:RU003903};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       proline from L-glutamate 5-semialdehyde: step 1/1.
CC       {ECO:0000256|HAMAP-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
CC       family. {ECO:0000256|HAMAP-Rule:MF_01925,
CC       ECO:0000256|RuleBase:RU003903}.
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DR   EMBL; CP000075; AAY35546.1; -; Genomic_DNA.
DR   RefSeq; WP_011266426.1; NC_007005.1.
DR   RefSeq; YP_233584.1; NC_007005.1.
DR   STRING; 205918.Psyr_0476; -.
DR   EnsemblBacteria; AAY35546; AAY35546; Psyr_0476.
DR   GeneID; 3365952; -.
DR   KEGG; psb:Psyr_0476; -.
DR   PATRIC; fig|205918.7.peg.495; -.
DR   eggNOG; ENOG4105II7; Bacteria.
DR   eggNOG; COG0345; LUCA.
DR   HOGENOM; HOG000230246; -.
DR   KO; K00286; -.
DR   OMA; FYFIEAM; -.
DR   BioCyc; PSYR205918:G1G4J-477-MONOMER; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000000426; 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   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;
DR   PRODOM; Q4ZZ76.
DR   SWISS-2DPAGE; Q4ZZ76.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01925, ECO:0000256|RuleBase:RU003903};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903, ECO:0000313|EMBL:AAY35546.1};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903}.
FT   DOMAIN        5     99       F420_oxidored. {ECO:0000259|Pfam:
FT                                PF03807}.
FT   DOMAIN      162    266       P5CR_dimer. {ECO:0000259|Pfam:PF14748}.
SQ   SEQUENCE   272 AA;  28005 MW;  97B5A2247263C7C1 CRC64;
     MSKTRIAFVG AGNMAASLIG GLRAQGVEAA LISASAPGAE TRERIANDHG IQVFADNADA
     IKGVDVVVLA VKPQMMKTVC QALKSGLEPH QLIVSVAAGI TCASLTQWLG EQPVVRCMPN
     TPSLLRQGAS GLYATDNVTP EQREQAEALL AAVGIAVWVE QEKHMDAVTA VSGSGPAYFF
     LMMEAMTAAG VKLGLPEDIA KKLTLQTALG SALIATGSDA GAGELRRRVT SPGGTTEAAI
     KAFQAGGFEA LVETALTAAD HRAAELAEQL GK
//

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