ID K4FSC8_CALMI Unreviewed; 271 AA.
AC K4FSC8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Pyrroline-5-carboxylate reductase 3 {ECO:0000256|ARBA:ARBA00039786};
DE EC=1.5.1.2 {ECO:0000256|ARBA:ARBA00012855};
DE AltName: Full=Pyrroline-5-carboxylate reductase-like protein {ECO:0000256|ARBA:ARBA00042532};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFK10913.1};
RN [1] {ECO:0000313|EMBL:AFK10913.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Intestine {ECO:0000313|EMBL:AFK10913.1};
RX PubMed=23056606;
RA Tan Y.Y., Kodzius R., Tay B.H., Tay A., Brenner S., Venkatesh B.;
RT "Sequencing and Analysis of Full-Length cDNAs, 5'-ESTs and 3'-ESTs from a
RT Cartilaginous Fish, the Elephant Shark (Callorhinchus milii).";
RL PLoS ONE 7:E47174-E47174(2012).
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 -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005205}.
CC -!- SUBUNIT: Homodecamer; composed of 5 homodimers.
CC {ECO:0000256|ARBA:ARBA00038523}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000256|ARBA:ARBA00005525}.
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DR EMBL; JX052685; AFK10913.1; -; mRNA.
DR AlphaFoldDB; K4FSC8; -.
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:SF71; PYRROLINE-5-CARBOXYLATE REDUCTASE 3; 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.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW NADP {ECO:0000256|PIRSR:PIRSR000193-1};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650}.
FT DOMAIN 8..101
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 59
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 271 AA; 28744 MW; BD06A95FB25A36FD CRC64;
MMDMEAMVGF VGAGTMAFAI ASGLVKADNV HRGNVMGSAP SDKNLIQFKN AGMQTTHCNE
SVLRSCSVIF LTIKPNILPT VLGEIYSLVT PEHLLISVAA GITVQTLEKL LPAGTRVLRT
MPNLACQVQE GTMVFCRGSH ATEQDASHLQ RLMSGCSLCE ETPEAFINIH SGLSGSGVAY
AYMFAEALAD GGVKMGMPYH LSLRLAGQTL VGAGKMMLET GEHPAKLKGD VRTPGGTTIH
AIHELERGNL RSTVMNAVEA ATNQARNMGK S
//
