ID A0A1V2LSB5_PICKU Unreviewed; 281 AA.
AC A0A1V2LSB5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|RuleBase:RU003903};
DE EC=1.5.1.2 {ECO:0000256|RuleBase:RU003903};
GN ORFNames=BOH78_1221 {ECO:0000313|EMBL:ONH76456.1}, C5L36_0C10780
GN {ECO:0000313|EMBL:AWU77173.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:ONH76456.1, ECO:0000313|Proteomes:UP000189274};
RN [1] {ECO:0000313|Proteomes:UP000189274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129 {ECO:0000313|Proteomes:UP000189274};
RX PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT Zimbabwe.";
RL Genome Announc. 5:E00064-E00064(2017).
RN [2] {ECO:0000313|EMBL:ONH76456.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129 {ECO:0000313|EMBL:ONH76456.1};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AWU77173.1, ECO:0000313|Proteomes:UP000249293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS573 {ECO:0000313|EMBL:AWU77173.1,
RC ECO:0000313|Proteomes:UP000249293};
RA Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A.,
RA Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.;
RT "Population genomics shows no distinction between pathogenic Candida krusei
RT and environmental Pichia kudriavzevii: One species, four names.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU003903};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC {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 EMBL; CP028775; AWU77173.1; -; Genomic_DNA.
DR EMBL; MQVM01000004; ONH76456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2LSB5; -.
DR STRING; 4909.A0A1V2LSB5; -.
DR VEuPathDB; FungiDB:C5L36_0C10780; -.
DR OrthoDB; 196930at2759; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000189274; Unassembled WGS sequence.
DR Proteomes; UP000249293; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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|RuleBase:RU003903};
KW Membrane {ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000193-1};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003903};
KW Proline biosynthesis {ECO:0000256|RuleBase:RU003903};
KW Reference proteome {ECO:0000313|Proteomes:UP000249293};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..108
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 174..277
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 12..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 41
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 66
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 281 AA; 29415 MW; CCA02973A0330E4D CRC64;
MQIPENYTLT ILGAGVMGSA VLSAVLKNRP TPFPGKIFCC TGSSASAQRL QETYGNAITA
TYGESNFQPV KEADVIVLGC KPFMCQTIID QVKGALDGNK VIISLLAGWK IDQLSTSVGS
PYIARVMTNT PAKYGCGTAV VSFSSDLQGT DFQSVRETIM AIVDTVGMAL ELPEKNMDAA
TSLVGSGPAF VLLMMQALAE GGVRMGIPYE TAKKCAAKVM EGTSKMVMES GQHPEALKSM
VCTPGGTTIG GLLTLEDRGV RGAISRAVEE AADIASKLGK K
//
