ID A0A5F9DM15_RABIT Unreviewed; 246 AA.
AC A0A5F9DM15;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Pyrroline-5-carboxylate reductase 2 {ECO:0000256|ARBA:ARBA00039795};
DE EC=1.5.1.2 {ECO:0000256|ARBA:ARBA00012855};
GN Name=PYCR2 {ECO:0000313|Ensembl:ENSOCUP00000047352.1};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000047352.1, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000047352.1, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000047352.1,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000047352.1}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000047352.1};
RG Ensembl;
RL Submitted (NOV-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 -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005205}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000256|ARBA:ARBA00005525}.
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DR EMBL; AAGW02025896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A5F9DM15; -.
DR Ensembl; ENSOCUT00000047051.1; ENSOCUP00000047352.1; ENSOCUG00000001915.5.
DR GeneTree; ENSGT00950000183044; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000001811; Chromosome 16.
DR Bgee; ENSOCUG00000001915; Expressed in embryo and 17 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 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 PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR PANTHER; PTHR11645:SF61; PYRROLINE-5-CARBOXYLATE REDUCTASE 2; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT DOMAIN 3..98
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 107..194
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
SQ SEQUENCE 246 AA; 25823 MW; C3A01AA3B76E5FD5 CRC64;
MSVGFIGAGQ LACALARGFT AAGILSAHKI MASSPEMDLP TVSALRKMGV NLTRSNKETV
RHSDVLFLAV KPHIIPFILD EIGADVQPRH IVVSCAAGVT ISSVEKAFMA VDALADGGVK
MGLPRRLAVR LGAQALLGAA KMLLDSEDHP GQLKDNVCSP GGATIHALHF LESGGFRSLL
INAVEASCIR TRELQSMADQ EKISPAALKK TLLDRVKLES PMVSTLAPSS TGKLLTRNVA
PGGKKD
//
