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Database: UniProt
Entry: C3M957_SINFN
LinkDB: C3M957_SINFN
Original site: C3M957_SINFN 
ID   C3M957_SINFN            Unreviewed;       256 AA.
AC   C3M957;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Pyrroline-5-carboxylate reductase {ECO:0000313|EMBL:ACP26768.1};
DE            EC=1.5.1.2 {ECO:0000313|EMBL:ACP26768.1};
GN   Name=proC1 {ECO:0000313|EMBL:ACP26768.1};
GN   OrderedLocusNames=NGR_c30250 {ECO:0000313|EMBL:ACP26768.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP26768.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP26768.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525}.
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DR   EMBL; CP001389; ACP26768.1; -; Genomic_DNA.
DR   RefSeq; YP_002827521.1; NC_012587.1.
DR   AlphaFoldDB; C3M957; -.
DR   STRING; 394.NGR_c30250; -.
DR   KEGG; rhi:NGR_c30250; -.
DR   PATRIC; fig|394.7.peg.5866; -.
DR   eggNOG; COG0345; Bacteria.
DR   HOGENOM; CLU_066353_0_0_5; -.
DR   OrthoDB; 9805754at2; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   Oxidoreductase {ECO:0000313|EMBL:ACP26768.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN          3..95
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          160..255
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         56
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         69..72
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   256 AA;  27520 MW;  48D7E02527459085 CRC64;
     MMRIGFVGTG TITEAMVTGI VGSDLGVEEI LVSPRNRQIA ARLASRFSSV RIAKDNQDVV
     DAADVLFLAV RPQIAEEVIT ALAFRAGQTV VSVIAATDRS KLLGWIREDV RLSQAIPLPF
     VAERAGVTAI YPPNPEIAAI FAALGSAVEC EAKEEYDLLA VASALMGTYF GILDRATGWV
     AEKGVAREKV RAYLAPLFAS LAQTAVRAET TPLDTLRREF STPGGLNEQV FDDFERGGGG
     RALTDALEAV LRRVRR
//
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