P5CR_AQUAE
ID P5CR_AQUAE Reviewed; 265 AA.
AC O66553;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000255|HAMAP-Rule:MF_01925};
DE Short=P5C reductase {ECO:0000255|HAMAP-Rule:MF_01925};
DE Short=P5CR {ECO:0000255|HAMAP-Rule:MF_01925};
DE EC=1.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01925};
DE AltName: Full=PCA reductase {ECO:0000255|HAMAP-Rule:MF_01925};
GN Name=proC {ECO:0000255|HAMAP-Rule:MF_01925}; OrderedLocusNames=aq_166;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC L-proline. {ECO:0000255|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: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}.
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; AE000657; AAC06504.1; -; Genomic_DNA.
DR PIR; F70315; F70315.
DR RefSeq; NP_213113.1; NC_000918.1.
DR RefSeq; WP_010880051.1; NC_000918.1.
DR AlphaFoldDB; O66553; -.
DR SMR; O66553; -.
DR STRING; 224324.aq_166; -.
DR EnsemblBacteria; AAC06504; AAC06504; aq_166.
DR KEGG; aae:aq_166; -.
DR PATRIC; fig|224324.8.peg.142; -.
DR eggNOG; COG0345; Bacteria.
DR HOGENOM; CLU_042344_3_1_0; -.
DR InParanoid; O66553; -.
DR OMA; VVRVMTN; -.
DR OrthoDB; 1349288at2; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000000798; 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..265
FT /note="Pyrroline-5-carboxylate reductase"
FT /id="PRO_0000187284"
SQ SEQUENCE 265 AA; 28814 MW; 32DD6B49EDDCF403 CRC64;
MHAIILTMRV GIVGFGNMGQ AFALCFSKKL GKENIIVTDK VQEKRNLATE MGIAFASDVK
FLADNSDVVL VAVKPKDSQE VLQKLKDYKG IILSIMAGVS IEKMEKILGK DKKIVRVMPN
VNVAVGSGVM AITDNGNLSE EERSKVEELL LSCGTLYRIE ERLFDAFTAL AGSGPAFVFS
FIDALALAGV HQGFSYEQAL RIALDTVMGS AKLLKEFQVN PNELIAKVTS PGGTTIEGIK
YLEEKGFKGT VMECINRTSQ KAKKL