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Database: UniProt
Entry: A0A157ZKN9_9BURK
LinkDB: A0A157ZKN9_9BURK
Original site: A0A157ZKN9_9BURK 
ID   A0A157ZKN9_9BURK        Unreviewed;       256 AA.
AC   A0A157ZKN9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Pyrroline-5-carboxylate reductase {ECO:0000313|EMBL:SAK45507.1};
GN   ORFNames=AWB75_00791 {ECO:0000313|EMBL:SAK45507.1};
OS   Caballeronia catudaia.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777136 {ECO:0000313|EMBL:SAK45507.1, ECO:0000313|Proteomes:UP000054870};
RN   [1] {ECO:0000313|EMBL:SAK45507.1, ECO:0000313|Proteomes:UP000054870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29318 {ECO:0000313|EMBL:SAK45507.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525}.
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DR   EMBL; FCOF02000003; SAK45507.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A157ZKN9; -.
DR   OrthoDB; 4425838at2; -.
DR   Proteomes; UP000054870; 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}.
FT   DOMAIN          3..95
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          152..252
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         55
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         68..71
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   256 AA;  27360 MW;  7C0BDE5FE989E223 CRC64;
     MHIGFIGAGT ITRAIVTGMI RFGVPFERIV LSPRNADIAA QLAKMDSRVE VCESNQGVLD
     ASDVVCLAVV PQIAPDVLSS LAFEARHHVI SFIAGMSLDQ IRELVRRSAK VVRAVPLPAV
     AVGKGSTAIC PHDEIAAALF SPLGEAVEVD DEHQFDALSA VTATMASFFA LLEEQASWLV
     AQGLPYASAR SFLAGYHVGL AHETTQGDAP FSAMIGHAST PGGLNEQLWR ELSERGTFAH
     YAEALDRIMR RVQGRG
//
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