P5CR1_BOVIN
ID P5CR1_BOVIN Reviewed; 320 AA.
AC Q58DT4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Pyrroline-5-carboxylate reductase 1, mitochondrial;
DE Short=P5C reductase 1;
DE Short=P5CR 1;
DE EC=1.5.1.2;
GN Name=PYCR1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Housekeeping enzyme that catalyzes the last step in proline
CC biosynthesis. Can utilize both NAD and NADP, but has higher affinity
CC for NAD. Involved in the cellular response to oxidative stress.
CC {ECO:0000250|UniProtKB:P32322}.
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:0000250|UniProtKB:P32322};
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:0000250|UniProtKB:P32322};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC -!- SUBUNIT: Homodecamer; composed of 5 homodimers. Interacts with LTO1.
CC {ECO:0000250|UniProtKB:P32322}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P32322}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT021513; AAX46360.1; -; mRNA.
DR EMBL; BC123510; AAI23511.1; -; mRNA.
DR RefSeq; NP_001014957.1; NM_001014957.1.
DR RefSeq; XP_010814772.1; XM_010816470.1.
DR AlphaFoldDB; Q58DT4; -.
DR SMR; Q58DT4; -.
DR STRING; 9913.ENSBTAP00000000046; -.
DR PaxDb; Q58DT4; -.
DR PeptideAtlas; Q58DT4; -.
DR PRIDE; Q58DT4; -.
DR Ensembl; ENSBTAT00000000046; ENSBTAP00000000046; ENSBTAG00000000042.
DR Ensembl; ENSBTAT00000075415; ENSBTAP00000064719; ENSBTAG00000000042.
DR GeneID; 539606; -.
DR KEGG; bta:539606; -.
DR CTD; 5831; -.
DR VEuPathDB; HostDB:ENSBTAG00000000042; -.
DR VGNC; VGNC:33586; PYCR1.
DR eggNOG; KOG3124; Eukaryota.
DR GeneTree; ENSGT00950000183044; -.
DR HOGENOM; CLU_042344_3_0_1; -.
DR InParanoid; Q58DT4; -.
DR OMA; VVRVMTN; -.
DR OrthoDB; 952695at2759; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000000042; Expressed in saliva-secreting gland and 104 other tissues.
DR ExpressionAtlas; Q58DT4; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006561; P:proline biosynthetic process; ISS:UniProtKB.
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 PANTHER; PTHR11645; PTHR11645; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00112; proC; 1.
DR PROSITE; PS00521; P5CR; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Amino-acid biosynthesis; Mitochondrion; NADP; Oxidoreductase;
KW Phosphoprotein; Proline biosynthesis; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P32322"
FT CHAIN 2..320
FT /note="Pyrroline-5-carboxylate reductase 1, mitochondrial"
FT /id="PRO_0000270817"
FT REGION 292..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 6..11
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 69..72
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 95..97
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P32322"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32322"
SQ SEQUENCE 320 AA; 33454 MW; 0265F89F283CA765 CRC64;
MSVGFIGAGQ LAFALAKGFT AAGVVAAHKI MASSPDMDLA TVSALRKMGV NLTHHNKETV
QHSDVLFLAV KPHIIPFILD EIAANIEARH IVVSCAAGVT ISSIEKKLTA FQPAPKVIRC
MTNTPVVVRE GATVYATGTH AQVEDGRLLE QLMSSVGFCT EVEEDLIDAV TGLSGSGPAY
AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLDS EQHPGQLKDN VCSPGGATIH
ALHVLESGGF RSLLIKAVEA SCTRTRELQS MADQEKVSPA AIKKTILDKV KLDSPPGTSL
APSGHSKLLP RSMAPAGKQD
