PUT2_YEAST
ID PUT2_YEAST Reviewed; 575 AA.
AC P07275; D3DKY4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial;
DE Short=P5C dehydrogenase;
DE EC=1.2.1.88;
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
DE Flags: Precursor;
GN Name=PUT2; OrderedLocusNames=YHR037W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6098824; DOI=10.1128/mcb.4.12.2837-2842.1984;
RA Krzywicki K.A., Brandriss M.C.;
RT "Primary structure of the nuclear PUT2 gene involved in the mitochondrial
RT pathway for proline utilization in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 4:2837-2842(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
RX PubMed=3062363; DOI=10.1128/mcb.8.11.4634-4641.1988;
RA Siddiqui A.H., Brandriss M.C.;
RT "A regulatory region responsible for proline-specific induction of the
RT yeast PUT2 gene is adjacent to its TATA box.";
RL Mol. Cell. Biol. 8:4634-4641(1988).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11502169}.
CC -!- INDUCTION: By proline and is regulated by a common control element
CC encoded by the PUT3 gene.
CC -!- MISCELLANEOUS: Present with 17200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M10029; AAA34924.1; -; Genomic_DNA.
DR EMBL; M22785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00062; AAB68907.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06728.1; -; Genomic_DNA.
DR PIR; S46738; RDBYC.
DR RefSeq; NP_011902.1; NM_001179167.1.
DR PDB; 4OE4; X-ray; 2.17 A; A/B=23-575.
DR PDB; 4OE6; X-ray; 1.95 A; A/B=23-575.
DR PDBsum; 4OE4; -.
DR PDBsum; 4OE6; -.
DR AlphaFoldDB; P07275; -.
DR SMR; P07275; -.
DR BioGRID; 36468; 112.
DR IntAct; P07275; 3.
DR STRING; 4932.YHR037W; -.
DR MaxQB; P07275; -.
DR PaxDb; P07275; -.
DR PRIDE; P07275; -.
DR EnsemblFungi; YHR037W_mRNA; YHR037W; YHR037W.
DR GeneID; 856432; -.
DR KEGG; sce:YHR037W; -.
DR SGD; S000001079; PUT2.
DR VEuPathDB; FungiDB:YHR037W; -.
DR eggNOG; KOG2455; Eukaryota.
DR GeneTree; ENSGT00560000077335; -.
DR HOGENOM; CLU_005391_4_1_1; -.
DR InParanoid; P07275; -.
DR OMA; FAGIHFT; -.
DR BioCyc; MetaCyc:YHR037W-MON; -.
DR BioCyc; YEAST:YHR037W-MON; -.
DR BRENDA; 1.2.1.88; 984.
DR UniPathway; UPA00261; UER00374.
DR PRO; PR:P07275; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P07275; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IDA:SGD.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006537; P:glutamate biosynthetic process; IDA:SGD.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IMP:SGD.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005931; P5CDH/ALDH4A1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01236; D1pyr5carbox1; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane; NAD;
KW Oxidoreductase; Proline metabolism; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..575
FT /note="Delta-1-pyrroline-5-carboxylate dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000007177"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 351
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 297..302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 212
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 187..188
FT /note="ES -> SR (in Ref. 1; AAA34924)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="P -> L (in Ref. 1; AAA34924)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="D -> G (in Ref. 1; AAA34924)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="N -> S (in Ref. 1; AAA34924)"
FT /evidence="ECO:0000305"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4OE6"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 99..117
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 121..136
FT /evidence="ECO:0007829|PDB:4OE6"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 164..180
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 289..305
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 361..377
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 405..418
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 443..449
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 461..469
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 474..483
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 498..507
FT /evidence="ECO:0007829|PDB:4OE6"
FT TURN 508..510
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:4OE6"
FT HELIX 548..552
FT /evidence="ECO:0007829|PDB:4OE6"
FT STRAND 553..560
FT /evidence="ECO:0007829|PDB:4OE6"
SQ SEQUENCE 575 AA; 64435 MW; 5A610D67985291B0 CRC64;
MLSARCLKSI YFKRSFSQLG HIKPPKHIRN EPVKPFRNID LKDWDLLRAS LMKFKSSSLE
VPLVINGERI YDNNERALFP QTNPANHQQV LANVTQATEK DVMNAVKAAK DAKKDWYNLP
FYDRSAIFLK AADLISTKYR YDMLAATMLG QGKNVYQAEI DCITELSDFF RYYVKYASDL
YAQQPVESAD GTWNKAEYRP LEGFVYAVSP FNFTAIAANL IGAPALMGNT VVWKPSQTAA
LSNYLLMTVL EEAGLPKGVI NFIPGDPVQV TDQVLADKDF GALHFTGSTN VFKSLYGKIQ
SGVVEGKYRD YPRIIGETGG KNFHLVHPSA NISHAVLSTI RGTFEFQGQK CSAASRLYLP
ESKSEEFLSD MFGILQSQNV VPMNTSASPI SGGNLRGFMG PVIHEQSFDK LVKVIEDAKK
DPELEILYGG QYDKSQGWFV GPTVIKAKRP DHPYMSTEFF GPILTVYEYP DTEFNEICDI
IDNTSQYALT GAIFAKDRKA IEYADEKLKF SAGNFYINDK CTGAVVSQQW FGGARMSGTD
DKAGGPNILS RFVSIRNTKE NFYELTDFKY PSNYE
