ID A0A2D8PCY1_9RHOB Unreviewed; 251 AA.
AC A0A2D8PCY1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Pyrroline-5-carboxylate reductase {ECO:0000313|EMBL:MAM63307.1};
GN ORFNames=CMH11_17635 {ECO:0000313|EMBL:MAM63307.1};
OS Maritimibacter sp.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=2003363 {ECO:0000313|EMBL:MAM63307.1, ECO:0000313|Proteomes:UP000224593};
RN [1] {ECO:0000313|Proteomes:UP000224593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Graham E.D., Heidelberg J.F.;
RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT Global Oceans.";
RL Submitted (SEP-2017) 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:MAM63307.1}.
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DR EMBL; NZNT01000029; MAM63307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D8PCY1; -.
DR Proteomes; UP000224593; 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; 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.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000193-1}.
FT DOMAIN 2..83
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 146..248
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 6..11
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 251 AA; 25459 MW; 2E9F8B67FA3F4EAC CRC64;
MKYGLIGSGM LGGALAKAAH ASGLDLMVAN RSGQSPVEGL PVTTDPQAVV EACDAVVLCV
PPASAGEIAM RARDTLVVSV MAGIPRDQIC ALTGSPRVVR AMSSPAAGLG LAYSPWCASA
SVTAADRAMI SAFFGACGET DEVPDEAQIE LFTAMTGPVP GFVAQFAASM VTYATERGVD
PDVADRAVRQ LFHASGVMMS TGPSPADHVQ EMVEYAGTTA AGLLALQATT LDEDIATGLD
AAVQKTRALG G
//