P5CR1_DICDI
ID P5CR1_DICDI Reviewed; 551 AA.
AC Q54IL7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Pyrroline-5-carboxylate reductase 1;
DE Short=P5C reductase 1;
DE Short=P5CR 1;
DE EC=1.5.1.2;
GN Name=pycr1; ORFNames=DDB_G0288671;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- 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 -!- 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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000119; EAL63112.1; -; Genomic_DNA.
DR RefSeq; XP_636614.1; XM_631522.1.
DR AlphaFoldDB; Q54IL7; -.
DR SMR; Q54IL7; -.
DR STRING; 44689.DDB0232206; -.
DR PaxDb; Q54IL7; -.
DR EnsemblProtists; EAL63112; EAL63112; DDB_G0288671.
DR GeneID; 8626742; -.
DR KEGG; ddi:DDB_G0288671; -.
DR dictyBase; DDB_G0288671; -.
DR eggNOG; KOG3124; Eukaryota.
DR HOGENOM; CLU_494711_0_0_1; -.
DR InParanoid; Q54IL7; -.
DR OMA; QSMTCLA; -.
DR PhylomeDB; Q54IL7; -.
DR Reactome; R-DDI-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00361.
DR PRO; PR:Q54IL7; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IBA:GO_Central.
DR GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
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 SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; NADP; Oxidoreductase; Proline biosynthesis;
KW Reference proteome.
FT CHAIN 1..551
FT /note="Pyrroline-5-carboxylate reductase 1"
FT /id="PRO_0000328304"
FT REGION 279..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 63009 MW; 6D15ED4680D6244D CRC64;
MKLYDNGVAV LGCGNLGNAI AKGLVASKQF KSNQIVLTKR NLSTIEPLKR EGYHVTTSNH
DAVSRCKIVI VCVVPAQLDD LLDSIKQSVT ENHIIISVVS GASIEDIRSH LEKDVPIVRA
MPNTAIQHCQ SMTCLAIRSS HQKSTNSPSD KAKDNALEVA KKIFNCLGMS IVLSEEQIVP
ATALCACGIA FFCRAIRAAA QGGCEIGFHA EDAIRIAAQT AKGAATLLLE NNFHPEYEID
KVTTPQGCTI AGLNQMEHAG FSSAMIKGIV TSSDKAASLY TQKQQNKKQQ QLKQQQHQQH
QHQQHQQHQQ QVQQQEPHQY QQQQQQSHQQ SQYNQGHNYG HQNQHHHNHD DQHQNYYNQD
QKRRNNRKHR SNENYDNHHH HNQQYQQHQQ PTQQESQEQT QQPEQTQSTN QSNQRRNSES
RNGKSPQKQP QKQSQVQQPS STTENTDQQQ QQQPPQEQQQ QQEQPQQPQE QQQQPNVVDE
AERPKEQQQQ PQQQQQTIDK KGYNNNRRGG RHYSYNNNYN SHHHRHNGIN KNSSSMYHDE
KRHEVKTEQI N
