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Database: UniProt
Entry: A0A2Y9JAT6_ENHLU
LinkDB: A0A2Y9JAT6_ENHLU
Original site: A0A2Y9JAT6_ENHLU 
ID   A0A2Y9JAT6_ENHLU        Unreviewed;       564 AA.
AC   A0A2Y9JAT6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|RuleBase:RU003903};
DE            EC=1.5.1.2 {ECO:0000256|RuleBase:RU003903};
GN   Name=LOC111146747 {ECO:0000313|RefSeq:XP_022358137.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022358137.1};
RN   [1] {ECO:0000313|RefSeq:XP_022358137.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022358137.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Enzyme that catalyzes the last step in proline biosynthesis.
CC       Proline is synthesized from either glutamate or ornithine; both are
CC       converted to pyrroline-5-carboxylate (P5C), and then to proline via
CC       pyrroline-5-carboxylate reductases (PYCRs). PYCRL is exclusively linked
CC       to the conversion of ornithine to proline.
CC       {ECO:0000256|ARBA:ARBA00037662}.
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   -!- SUBUNIT: Homodecamer; composed of 5 homodimers.
CC       {ECO:0000256|ARBA:ARBA00038523}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525, ECO:0000256|RuleBase:RU003903}.
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DR   RefSeq; XP_022358137.1; XM_022502429.1.
DR   AlphaFoldDB; A0A2Y9JAT6; -.
DR   STRING; 391180.A0A2Y9JAT6; -.
DR   KEGG; elk:111146747; -.
DR   OrthoDB; 196930at2759; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000248482; Unplaced.
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 3; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 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|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU003903};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU003903};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003903};
KW   Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650,
KW   ECO:0000256|RuleBase:RU003903};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482}.
FT   DOMAIN          143..237
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          300..404
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   REGION          35..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  58749 MW;  95D875664004C012 CRC64;
     MSRWWGVGSG VQALPAPAFH QSQGECFLLE AKLPSSPRRS FPASAASSRG TPTRHAPGRR
     PPGQRGTPAL SDPSPLNGAS QAVHTTHPDP ATASSGPEQA ARRNGPADRW PIGWAEGVGR
     GTVGSGRGNM AAAVAEPGTS PLRVGFVGAG RMAEAIAQGF IRAGKVEARH ILASAPTDRN
     LCHFQALGCQ TTHSNREVLQ NCLLVFFATK PHVLPTVLAE VAPVVTSEHI LVSVAAGVSL
     STLEELLPPT ARVLRVSPNL PCVVQEGAMV MARGRHAGSS EAKLLQALLE ACGQCEEVPE
     AHVDIHTGLS GSGVAYVCAF SEALAEGAIK MGMPGSLAHR IAAQTLLGTA KMLQQNGQHP
     AQLRTDVCTP GGTTIYGLHA LERGGLRAAA MSAVEAATCR ARELSGKQGT APGRWQAQLT
     LTTDPWVILK GLLAWPLTEG RDSSAYPHME QPAGNARNLG PKPRPWGLWV DGGLPAAVPP
     HYPRGSWSSP TPPRPWSAGT ALAPACRPAD ARPPRGGVCS QSVRRVVAGD TLQQCSPAPA
     LHPQPGLPRT SPGASAPDRP GRRE
//
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