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Database: UniProt
Entry: A0A1S3S0Z2_SALSA
LinkDB: A0A1S3S0Z2_SALSA
Original site: A0A1S3S0Z2_SALSA 
ID   A0A1S3S0Z2_SALSA        Unreviewed;       320 AA.
AC   A0A1S3S0Z2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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};
GN   Name=LOC106606436 {ECO:0000313|RefSeq:XP_014058111.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014058111.1};
RN   [1] {ECO:0000313|RefSeq:XP_014058111.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014058111.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_014058111.1; XM_014202636.1.
DR   AlphaFoldDB; A0A1S3S0Z2; -.
DR   STRING; 8030.ENSSSAP00000047503; -.
DR   PaxDb; 8030-ENSSSAP00000047503; -.
DR   Ensembl; ENSSSAT00000074773; ENSSSAP00000047477; ENSSSAG00000048220.
DR   GeneID; 106606436; -.
DR   KEGG; sasa:106606436; -.
DR   OMA; RPYRAMT; -.
DR   OrthoDB; 196930at2759; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000087266; Chromosome ssa06.
DR   Bgee; ENSSSAG00000048220; Expressed in muscle tissue and 15 other cell types or tissues.
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:SF63; 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|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU003903};
KW   NADP {ECO:0000256|PIRSR:PIRSR000193-1, 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:UP000087266}.
FT   DOMAIN          3..98
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          164..268
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         34
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
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"
FT   BINDING         95..97
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   320 AA;  33750 MW;  3D6155FE48F53D6C CRC64;
     MSVGFIGAGQ LAHALVKGFS AAGVIATQRI TASSPDTDLP TVSGLRKMGV NLTTSNKEVV
     NKSDVLFLAV KPHIIPFVLD EIGPDIEDRH LIVSCAAGVT ISSIEKKLLQ YRPFPKVMRC
     MTNTPVVVRE GATVYATGTH AELEDGRLLE QLMASVGYCT EVEEDLIDAV TGLSGSGPAY
     AFTAVEALAD GGVKMGLPRR LAIRLGAQAL LGAAKMLLDS EQHPGQLKDN VCSPGGATIH
     ALHVMESGGF RSLLINAVEA SCIRTRELQF LADQEKISPA AIKKTTLDKV LQQPGVGKGV
     GVRTGSGISL FSSSNPRHKK
//
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