(data stored in SCRATCH zone)

SWISSPROT: Q145H2_PARXL

ID   Q145H2_PARXL            Unreviewed;       271 AA.
AC   Q145H2;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 94.
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   ORFNames=Bxe_A3982 {ECO:0000313|EMBL:ABE29017.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29017.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29017.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29017.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000270; ABE29017.1; -; Genomic_DNA.
DR   RefSeq; WP_011486840.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A3982; -.
DR   EnsemblBacteria; ABE29017; ABE29017; Bxe_A3982.
DR   GeneID; 4004611; -.
DR   KEGG; bxb:DR64_1658; -.
DR   KEGG; bxe:Bxe_A3982; -.
DR   PATRIC; fig|266265.5.peg.507; -.
DR   eggNOG; ENOG4105II7; Bacteria.
DR   eggNOG; COG0345; LUCA.
DR   HOGENOM; HOG000230246; -.
DR   KO; K00286; -.
DR   OMA; FYFIEAM; -.
DR   OrthoDB; 1349288at2; -.
DR   BioCyc; BXEN266265:BXE_RS02400-MONOMER; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000001817; Chromosome 1.
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; Q145H2.
DR   SWISS-2DPAGE; Q145H2.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
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:ABE29017.1};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        2     96       F420_oxidored. {ECO:0000259|Pfam:
FT                                PF03807}.
FT   DOMAIN      160    264       P5CR_dimer. {ECO:0000259|Pfam:PF14748}.
SQ   SEQUENCE   271 AA;  27820 MW;  1149773E1FA27E9B CRC64;
     MKIAFIGGGN MAAALIGGLI KRGVAAADLY AIDPNEEARK RNEQQFGIRT GAAADAALAA
     YDAVVLAVKP QILKSVAEAV APHLNASQLV VSIVAGIRMG DMSRWLNGHS RIVRVMPNTP
     ALIGMGVTGL VATGSVDEAG RALASQLLGA VGETVWFDDE AKIDAVTAIS GSGPAYVFYF
     IEALQEAARQ LGMDEAQGRA LAVATFTGAA QLAANSDEPP GVLRERVTSK GGTTAAALAS
     FDASGIKDAI VRGALAANAR AREMGDEFGK Q
//

If you have problems or comments...

PBIL Back to PBIL home page