P5CR_PSEAE
ID P5CR_PSEAE Reviewed; 273 AA.
AC P22008;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000255|HAMAP-Rule:MF_01925};
DE Short=P5C reductase {ECO:0000255|HAMAP-Rule:MF_01925, ECO:0000303|PubMed:2107123};
DE Short=P5CR {ECO:0000255|HAMAP-Rule:MF_01925};
DE EC=1.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01925, ECO:0000269|PubMed:2107123};
DE AltName: Full=PCA reductase {ECO:0000255|HAMAP-Rule:MF_01925};
GN Name=proC {ECO:0000255|HAMAP-Rule:MF_01925, ECO:0000303|PubMed:2107123};
GN OrderedLocusNames=PA0393;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=2107123; DOI=10.1016/0378-1119(90)90121-7;
RA Savioz A., Jeenes D.J., Kocher H.P., Haas D.;
RT "Comparison of proC and other housekeeping genes of Pseudomonas aeruginosa
RT with their counterparts in Escherichia coli.";
RL Gene 86:107-111(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1676385; DOI=10.1016/0378-1119(91)90221-v;
RA Whitchurch C.B., Hobbs M., Livingston S.P., Krishnapillai V., Mattick J.S.;
RT "Characterisation of a Pseudomonas aeruginosa twitching motility gene and
RT evidence for a specialised protein export system widespread in
RT eubacteria.";
RL Gene 101:33-44(1991).
CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC L-proline. {ECO:0000255|HAMAP-Rule:MF_01925,
CC ECO:0000269|PubMed:2107123}.
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 ECO:0000269|PubMed:2107123};
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 ECO:0000269|PubMed:2107123};
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01925}.
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DR EMBL; M33557; AAA25975.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03782.1; -; Genomic_DNA.
DR EMBL; M55524; AAA25958.1; -; Genomic_DNA.
DR PIR; JQ0418; JQ0418.
DR RefSeq; NP_249084.1; NC_002516.2.
DR RefSeq; WP_003114890.1; NZ_QZGE01000016.1.
DR AlphaFoldDB; P22008; -.
DR SMR; P22008; -.
DR STRING; 287.DR97_3361; -.
DR PaxDb; P22008; -.
DR PRIDE; P22008; -.
DR EnsemblBacteria; AAG03782; AAG03782; PA0393.
DR GeneID; 878413; -.
DR KEGG; pae:PA0393; -.
DR PATRIC; fig|208964.12.peg.414; -.
DR PseudoCAP; PA0393; -.
DR HOGENOM; CLU_042344_0_1_6; -.
DR InParanoid; P22008; -.
DR OMA; VVRVMTN; -.
DR PhylomeDB; P22008; -.
DR BioCyc; PAER208964:G1FZ6-397-MON; -.
DR SABIO-RK; P22008; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000002438; 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 GO; GO:0006561; P:proline biosynthetic process; TAS:PseudoCAP.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; Direct protein sequencing; NADP;
KW Oxidoreductase; Proline biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2107123"
FT CHAIN 2..273
FT /note="Pyrroline-5-carboxylate reductase"
FT /id="PRO_0000187296"
SQ SEQUENCE 273 AA; 28094 MW; 6B2D191635E8DEE0 CRC64;
MSTPRIAFIG AGNMAASLIG GLRAQGVPAA QIRASDPGAE QRAKIAGEFA IDVVESNAEA
VADADVVVLS VKPQAMKAVC QALAPALKPE QLIVSIAAGI PCASLEAWLG QPRPVVRCMP
NTPALLRQGA SGLYANAQVS AAQCEQAGQL LSAVGIALWL DDEAQIDAVT AVSGSGPAYF
FLLMQAMTDA GEKLGLSRET ASRLTLQTAL GAAQMALSSE VEPAELRRRV TSPNGTTEAA
IKSFQANGFE ALVEQALNAA SQRSAELAEQ LGQ
