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Database: UniProt
Entry: I6YJF7_TIGCA
LinkDB: I6YJF7_TIGCA
Original site: I6YJF7_TIGCA 
ID   I6YJF7_TIGCA            Unreviewed;       269 AA.
AC   I6YJF7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|ARBA:ARBA00012855, ECO:0000256|RuleBase:RU003903};
DE            EC=1.5.1.2 {ECO:0000256|ARBA:ARBA00012855, ECO:0000256|RuleBase:RU003903};
DE   Flags: Fragment;
GN   Name=P5CR {ECO:0000313|EMBL:AFN54322.1};
OS   Tigriopus californicus (Marine copepod).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Hexanauplia; Copepoda; Harpacticoida; Harpacticidae; Tigriopus.
OX   NCBI_TaxID=6832 {ECO:0000313|EMBL:AFN54322.1};
RN   [1] {ECO:0000313|EMBL:AFN54322.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LJSf19_a {ECO:0000313|EMBL:AFN54321.1}, and LJSf19_b
RC   {ECO:0000313|EMBL:AFN54322.1};
RX   PubMed=22760646; DOI=10.1007/s00239-012-9508-1;
RA   Willett C.S.;
RT   "Quantifying the Elevation of Mitochondrial DNA Evolutionary Substitution
RT   Rates Over Nuclear Rates in the Intertidal Copepod Tigriopus
RT   californicus.";
RL   J. Mol. Evol. 0:0-0(2012).
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|ARBA:ARBA00000593};
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|ARBA:ARBA00000723,
CC         ECO:0000256|RuleBase:RU003903};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC       from L-glutamate 5-semialdehyde: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005205, ECO:0000256|RuleBase:RU003903}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525, ECO:0000256|RuleBase:RU003903}.
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DR   EMBL; JQ966497; AFN54321.1; -; Genomic_DNA.
DR   EMBL; JQ966498; AFN54322.1; -; Genomic_DNA.
DR   AlphaFoldDB; I6YJF7; -.
DR   UniPathway; UPA00098; UER00361.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-EC.
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|RuleBase:RU003903};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000193-1};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003903};
KW   Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650,
KW   ECO:0000256|RuleBase:RU003903}.
FT   DOMAIN          6..102
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          165..268
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         10..15
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         61
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         74..77
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFN54322.1"
FT   NON_TER         269
FT                   /evidence="ECO:0000313|EMBL:AFN54322.1"
SQ   SEQUENCE   269 AA;  28365 MW;  9319E994EAEF8220 CRC64;
     MGANLRVGFI GAGKMASALA QGFIKGQAVK CASHVSASCP IADKHLLEHM KQMGCQTFHC
     NKELMDCSDV VILAVKPQIM PLVLPDIKSL VASKLMVSIA AGVQLAQLQA DLNPDSKIVR
     LMPNTPCIVR EGVSVFCSGP QVTPQDNATV KQLFGTVGQI DEVKESMIDA VTGVSGSGPA
     YMYLIIEAMA DGGVKQGLPR DLAYKLAAQT MVGAGRMVLD THTHPAVLKD EVCSPGGTTI
     TALDMLEKSG LRTSIMQAVE AATKRCTQI
//
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