GenomeNet

Database: UniProt
Entry: W5WKJ7_9PSEU
LinkDB: W5WKJ7_9PSEU
Original site: W5WKJ7_9PSEU 
ID   W5WKJ7_9PSEU            Unreviewed;       268 AA.
AC   W5WKJ7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=KALB_8367 {ECO:0000313|EMBL:AHI01724.1};
OS   Kutzneria albida DSM 43870.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kutzneria.
OX   NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI01724.1, ECO:0000313|Proteomes:UP000019225};
RN   [1] {ECO:0000313|EMBL:AHI01724.1, ECO:0000313|Proteomes:UP000019225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI01724.1};
RX   PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA   Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA   Bechthold A., Kalinowski J., Luzhetskyy A.;
RT   "Complete genome sequence of producer of the glycopeptide antibiotic
RT   Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT   of Pseudonocardiaceae.";
RL   BMC Genomics 15:885-885(2014).
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}.
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; CP007155; AHI01724.1; -; Genomic_DNA.
DR   RefSeq; WP_025361516.1; NZ_CP007155.1.
DR   AlphaFoldDB; W5WKJ7; -.
DR   STRING; 1449976.KALB_8367; -.
DR   KEGG; kal:KALB_8367; -.
DR   PATRIC; fig|1449976.3.peg.8402; -.
DR   eggNOG; COG0345; Bacteria.
DR   HOGENOM; CLU_042344_0_0_11; -.
DR   OrthoDB; 9805754at2; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000019225; 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; IPR033379; Acid_Pase_AS.
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 3; 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; PS00616; HIS_ACID_PHOSPHAT_1; 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:UP000019225}.
FT   DOMAIN          3..96
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          159..263
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         67..70
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   268 AA;  27893 MW;  18988C19C23707C7 CRC64;
     MTTIAVLGAG KIGEALLSGL LHGGWSTADL MFTERYPQRC EELTARHGVR AVSVPDAAAT
     ADVLVVAVKP QDIEPLLGEL SPVLKPGALV VSLCAGLPTK LFERELPEGT PVVRVMPNTP
     MLVGEAMSAI SAGAHARPEH LELVEGLLGS VGKVLRVPES QQDAVTALSG SGPAYFFFLV
     EAMIDAGILL GLPRAVAAQL IIQSAVGAAT MLADSGEHPV TLREAVTSPA GTTIMAVREL
     ERHGVRAALL AAIEAARDRS EELGRAHD
//
DBGET integrated database retrieval system