P5CR3_BACSU
ID P5CR3_BACSU Reviewed; 272 AA.
AC Q00777;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Pyrroline-5-carboxylate reductase 3;
DE Short=P5C reductase 3;
DE Short=P5CR 3;
DE EC=1.5.1.2;
DE AltName: Full=PCA reductase 3;
GN Name=proG; Synonyms=ykeA, yzcA; OrderedLocusNames=BSU12910;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 247-272.
RC STRAIN=168;
RX PubMed=1766370; DOI=10.1111/j.1365-2958.1991.tb00814.x;
RA Mathiopoulos C., Mueller J.P., Slack F.J., Murphy C.G., Patankar S.,
RA Bukusoglu G., Sonenshein A.L.;
RT "A Bacillus subtilis dipeptide transport system expressed early during
RT sporulation.";
RL Mol. Microbiol. 5:1903-1913(1991).
RN [4]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=11418582; DOI=10.1128/jb.183.14.4389-4392.2001;
RA Belitsky B.R., Brill J., Bremer E., Sonenshein A.L.;
RT "Multiple genes for the last step of proline biosynthesis in Bacillus
RT subtilis.";
RL J. Bacteriol. 183:4389-4392(2001).
CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC L-proline. {ECO:0000305|PubMed:11418582}.
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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC {ECO:0000269|PubMed:11418582}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: The proG proH proI triple mutant is auxotrophic
CC for proline. {ECO:0000269|PubMed:11418582}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000305}.
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DR EMBL; AJ002571; CAA05571.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13148.1; -; Genomic_DNA.
DR EMBL; X56678; CAA40001.1; -; Genomic_DNA.
DR PIR; F69855; F69855.
DR RefSeq; NP_389174.1; NC_000964.3.
DR RefSeq; WP_003232626.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; Q00777; -.
DR SMR; Q00777; -.
DR STRING; 224308.BSU12910; -.
DR PaxDb; Q00777; -.
DR PRIDE; Q00777; -.
DR EnsemblBacteria; CAB13148; CAB13148; BSU_12910.
DR GeneID; 936776; -.
DR KEGG; bsu:BSU12910; -.
DR PATRIC; fig|224308.179.peg.1403; -.
DR eggNOG; COG0345; Bacteria.
DR OMA; NRNTHIV; -.
DR PhylomeDB; Q00777; -.
DR BioCyc; BSUB:BSU12910-MON; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IBA:GO_Central.
DR GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Proline biosynthesis; Reference proteome.
FT CHAIN 1..272
FT /note="Pyrroline-5-carboxylate reductase 3"
FT /id="PRO_0000187287"
SQ SEQUENCE 272 AA; 30203 MW; 3109430A67868638 CRC64;
MEQIGLIGYG SMADMIARQL LKHEQIKENE LFIETRTKGE RLRALMSDYP NVSADPLENW
ANTCQLILIC VPPLHVIETM RRLYPYVNRN THIVSIAAGV PLRLLEAETE AGISRVIPAI
TSEAEAGISL VVHSEALAAE KKERLNELLS VFSRVREIKE SNLDVASNLT SSAPGFIAAI
FEELALSAVR NSSLSKEEAF DFLIHSLYGT GKMLIEKNMS FEETLERVAT KGGITGEGAE
VIHASVPDVF DEVFERTLRK YELLTEQVGK QT
