ID U2J2N9_9STRE Unreviewed; 256 AA.
AC U2J2N9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=HMPREF1557_01914 {ECO:0000313|EMBL:ERJ74005.1};
OS Streptococcus sobrinus W1703.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1227275 {ECO:0000313|EMBL:ERJ74005.1, ECO:0000313|Proteomes:UP000016617};
RN [1] {ECO:0000313|EMBL:ERJ74005.1, ECO:0000313|Proteomes:UP000016617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1703 {ECO:0000313|EMBL:ERJ74005.1,
RC ECO:0000313|Proteomes:UP000016617};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:ERJ74005.1}.
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DR EMBL; AWVA01000116; ERJ74005.1; -; Genomic_DNA.
DR RefSeq; WP_019771300.1; NZ_KI259730.1.
DR AlphaFoldDB; U2J2N9; -.
DR PATRIC; fig|1227275.3.peg.1716; -.
DR HOGENOM; CLU_042344_3_1_9; -.
DR OrthoDB; 9805754at2; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000016617; Unassembled WGS sequence.
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 2..83
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 152..256
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"
FT BINDING 64..67
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 256 AA; 27221 MW; 403B77F36FDEFC9C CRC64;
MKIGFIGLGK MATAIIKGLE KTDFEILVAG RDPEKTARQA QELGVRALAQ HSELVTQADL
IVLAVKPQVL PSVLDKLTFH QPIMSMAAGV SLERLAELTD PSLPLIRIMP NINAQILQST
TAICRNQQVD DQLLDLAKTI TNSFGSTFEI AEKDFDSFTA LAGSSPAYIY LFMEALALAG
VKHGLPKDQA VDIVTQTVLA SAQNLSQGQD SPHDLMDKIS SPGGTTIAGL ADLEKTGLTA
SVISGIDATI ARAKEL
//
