ID A0A0Q5P495_9BURK Unreviewed; 267 AA.
AC A0A0Q5P495;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASG35_05875 {ECO:0000313|EMBL:KQR81809.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR81809.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR81809.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR81809.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR81809.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR81809.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000256|ARBA:ARBA00005525}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQR81809.1}.
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DR EMBL; LMPF01000012; KQR81809.1; -; Genomic_DNA.
DR RefSeq; WP_056357345.1; NZ_LMPF01000012.1.
DR AlphaFoldDB; A0A0Q5P495; -.
DR OrthoDB; 4425838at2; -.
DR Proteomes; UP000051826; Unassembled WGS sequence.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:InterPro.
DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
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 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:SF13; -; 1.
DR PANTHER; PTHR11645; 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.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|PIRSR:PIRSR000193-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051826}.
FT DOMAIN 7..99
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 157..251
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 59
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 72..75
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 267 AA; 29003 MW; 6735B5A4C116FC9F CRC64;
MTKPISLGFV GSGDITHAIV TGIFSQAQPR YEVWLSPRNA EISKELAARY SGVHVARDNQ
HVVDQTEIIF LAVRPQIAAD VLGALSFAPD QCVVSLIAGY GTEQVRDSLR NAPKRIVRAL
PLPMVAHAAS RTVLYPVETC VRDIFETIGG SLGVASEDQF DTMLALSASM GLFFATAHAQ
SSWASRKGVD YDDARSYLMS LCKGLADAAL RSDIPLDELS RQYSTSGGIN EQVVSLMAQA
DMFKKIDTVY DSIETRLAAT RKSNRSI
//