P5CR1_BACSU
ID P5CR1_BACSU Reviewed; 297 AA.
AC P0CI77; O07508; O31828; P14383;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Pyrroline-5-carboxylate reductase 1 {ECO:0000255|HAMAP-Rule:MF_01925};
DE Short=P5C reductase 1 {ECO:0000255|HAMAP-Rule:MF_01925};
DE Short=P5CR 1 {ECO:0000255|HAMAP-Rule:MF_01925};
DE EC=1.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01925};
DE AltName: Full=PCA reductase 1 {ECO:0000255|HAMAP-Rule:MF_01925};
GN Name=proH; Synonyms=proC, yoxE; OrderedLocusNames=BSU18480;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-297, FUNCTION, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / SMY;
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 Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01925};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01925, ECO:0000269|PubMed:11418582}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925}.
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:0000255|HAMAP-Rule:MF_01925}.
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; AL009126; CAB13741.2; -; Genomic_DNA.
DR EMBL; AF006720; AAB62697.1; -; Genomic_DNA.
DR PIR; E69682; E69682.
DR RefSeq; NP_389730.2; NC_000964.3.
DR RefSeq; WP_010886524.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P0CI77; -.
DR SMR; P0CI77; -.
DR STRING; 224308.BSU18480; -.
DR PaxDb; P0CI77; -.
DR PRIDE; P0CI77; -.
DR EnsemblBacteria; CAB13741; CAB13741; BSU_18480.
DR GeneID; 940035; -.
DR KEGG; bsu:BSU18480; -.
DR PATRIC; fig|224308.43.peg.1958; -.
DR eggNOG; COG0345; Bacteria.
DR InParanoid; P0CI77; -.
DR OMA; VVRVMTN; -.
DR PhylomeDB; P0CI77; -.
DR BioCyc; BSUB:BSU18480-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 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 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.
DR TIGRFAMs; TIGR00112; proC; 1.
DR PROSITE; PS00521; P5CR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Proline biosynthesis; Reference proteome.
FT CHAIN 1..297
FT /note="Pyrroline-5-carboxylate reductase 1"
FT /id="PRO_0000187285"
SQ SEQUENCE 297 AA; 32031 MW; F4DC7E6F84C6ED42 CRC64;
MRTKKRTKEM LPIFDQKKVA FIGAGSMAEG MISGIVRANK IPKQNICVTN RSNTERLTEL
ELQYGIKGAL PNQLCIEDMD VLILAMKPKD AENALSSLKS RIQPHQLILS VLAGITTSFI
EQSLLNEQPV VRVMPNTSSM IGASATAIAL GKYVSEDLKK LAEALLGCMG EVYTIQENQM
DIFTGIAGSG PAYFYYLMEF IEKTGEEAGL DKQLSRSIGA QTLLGAAKML METGEHPEIL
RDNITSPNGT TAAGLQALKK SGGGEAISQA IKHAAKRSKE ISEDIEKTAA PLSGVIK
