ID J9S8H3_9ACTN Unreviewed; 286 AA.
AC J9S8H3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=KTR9_0904 {ECO:0000313|EMBL:AFR47549.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR47549.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR47549.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR47549.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
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}.
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DR EMBL; CP002907; AFR47549.1; -; Genomic_DNA.
DR RefSeq; WP_014925540.1; NC_018581.1.
DR AlphaFoldDB; J9S8H3; -.
DR STRING; 337191.KTR9_0904; -.
DR KEGG; gor:KTR9_0904; -.
DR PATRIC; fig|337191.3.peg.1113; -.
DR eggNOG; COG0345; Bacteria.
DR HOGENOM; CLU_042344_3_1_11; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000003281; 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; 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; 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; 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}.
FT DOMAIN 4..87
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 163..264
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 68..71
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 286 AA; 29527 MW; 071FA9A06F19859D CRC64;
MSERIAIIGG GKIGEALLAG MIGAGTPTKD LVVAERQESR AAEIADEYGV LVTDVKSAAE
SAQYVFLAIK PDDVDSILRI LASAEDNAES ERVTVTLVAG LPLSRYESAL QAGSPVIRVM
PNTPMLVNEA MSAVSAGRYV GDEQLQAVVK ILQTVGRVTV VPEKQMDAVT AVSGSGPAYV
FLLAEAMIDA GVGLGLTRPQ ASEMAVQTIR GAGILLSDSG LSPVDLRAAV TSPGGTTAEA
IREFEANGLR HAVYQATRAC AAASARGGRR VEVEGLAQGH AVTDTP
//
