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Protein

Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial

Gene

PUT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH.

Pathwayi: L-proline degradation into L-glutamate

This protein is involved in step 2 of the subpathway that synthesizes L-glutamate from L-proline.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Proline dehydrogenase, mitochondrial (PUT1)
  2. Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (PUT2)
This subpathway is part of the pathway L-proline degradation into L-glutamate, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from L-proline, the pathway L-proline degradation into L-glutamate and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei212 – 2121Transition state stabilizerBy similarity
Active sitei317 – 3171Proton acceptorPROSITE-ProRule annotation
Active sitei351 – 3511NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi297 – 3026NADBy similarity

GO - Molecular functioni

GO - Biological processi

  • glutamate biosynthetic process Source: SGD
  • proline biosynthetic process Source: InterPro
  • proline catabolic process to glutamate Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Proline metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-646.
YEAST:YHR037W-MONOMER.
ReactomeiR-SCE-70688. Proline catabolism.
UniPathwayiUPA00261; UER00374.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (EC:1.2.1.88)
Short name:
P5C dehydrogenase
Alternative name(s):
L-glutamate gamma-semialdehyde dehydrogenase
Gene namesi
Name:PUT2
Ordered Locus Names:YHR037W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR037W.
SGDiS000001079. PUT2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: UniProtKB-SubCell
  • mitochondrial matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 575Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrialPRO_0000007177
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

MaxQBiP07275.

Expressioni

Inductioni

By proline and is regulated by a common control element encoded by the PUT3 gene.

Interactioni

Protein-protein interaction databases

BioGridi36468. 23 interactions.
IntActiP07275. 3 interactions.
MINTiMINT-640995.

Structurei

Secondary structure

1
575
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi44 – 5613Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 653Combined sources
Beta strandi68 – 703Combined sources
Turni73 – 753Combined sources
Beta strandi78 – 836Combined sources
Beta strandi86 – 9510Combined sources
Helixi99 – 11719Combined sources
Helixi121 – 13616Combined sources
Turni137 – 1393Combined sources
Helixi140 – 15112Combined sources
Helixi155 – 1628Combined sources
Helixi164 – 18017Combined sources
Beta strandi193 – 2008Combined sources
Beta strandi202 – 2087Combined sources
Helixi214 – 22613Combined sources
Beta strandi231 – 2344Combined sources
Helixi237 – 2393Combined sources
Helixi240 – 25213Combined sources
Beta strandi259 – 2624Combined sources
Helixi267 – 2748Combined sources
Beta strandi280 – 2878Combined sources
Helixi289 – 30517Combined sources
Beta strandi313 – 3175Combined sources
Beta strandi322 – 3265Combined sources
Helixi332 – 34413Combined sources
Helixi345 – 3484Combined sources
Beta strandi354 – 3607Combined sources
Helixi361 – 37717Combined sources
Helixi405 – 41814Combined sources
Beta strandi424 – 4285Combined sources
Beta strandi435 – 4373Combined sources
Beta strandi443 – 4497Combined sources
Helixi453 – 4553Combined sources
Beta strandi461 – 4699Combined sources
Helixi471 – 4733Combined sources
Helixi474 – 48310Combined sources
Beta strandi489 – 4946Combined sources
Helixi498 – 50710Combined sources
Turni508 – 5103Combined sources
Beta strandi513 – 5197Combined sources
Helixi548 – 5525Combined sources
Beta strandi553 – 5608Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OE4X-ray2.17A/B23-575[»]
4OE6X-ray1.95A/B23-575[»]
ProteinModelPortaliP07275.
SMRiP07275. Positions 43-565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00560000077335.
HOGENOMiHOG000271511.
InParanoidiP07275.
KOiK00294.
OMAiTDYRYPF.
OrthoDBiEOG7BCNMF.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005931. P5CDH/ALDH4A1.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01236. D1pyr5carbox1. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07275-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSARCLKSI YFKRSFSQLG HIKPPKHIRN EPVKPFRNID LKDWDLLRAS
60 70 80 90 100
LMKFKSSSLE VPLVINGERI YDNNERALFP QTNPANHQQV LANVTQATEK
110 120 130 140 150
DVMNAVKAAK DAKKDWYNLP FYDRSAIFLK AADLISTKYR YDMLAATMLG
160 170 180 190 200
QGKNVYQAEI DCITELSDFF RYYVKYASDL YAQQPVESAD GTWNKAEYRP
210 220 230 240 250
LEGFVYAVSP FNFTAIAANL IGAPALMGNT VVWKPSQTAA LSNYLLMTVL
260 270 280 290 300
EEAGLPKGVI NFIPGDPVQV TDQVLADKDF GALHFTGSTN VFKSLYGKIQ
310 320 330 340 350
SGVVEGKYRD YPRIIGETGG KNFHLVHPSA NISHAVLSTI RGTFEFQGQK
360 370 380 390 400
CSAASRLYLP ESKSEEFLSD MFGILQSQNV VPMNTSASPI SGGNLRGFMG
410 420 430 440 450
PVIHEQSFDK LVKVIEDAKK DPELEILYGG QYDKSQGWFV GPTVIKAKRP
460 470 480 490 500
DHPYMSTEFF GPILTVYEYP DTEFNEICDI IDNTSQYALT GAIFAKDRKA
510 520 530 540 550
IEYADEKLKF SAGNFYINDK CTGAVVSQQW FGGARMSGTD DKAGGPNILS
560 570
RFVSIRNTKE NFYELTDFKY PSNYE
Length:575
Mass (Da):64,435
Last modified:February 1, 1995 - v2
Checksum:i5A610D67985291B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1882ES → SR in AAA34924 (PubMed:6098824).Curated
Sequence conflicti264 – 2641P → L in AAA34924 (PubMed:6098824).Curated
Sequence conflicti541 – 5411D → G in AAA34924 (PubMed:6098824).Curated
Sequence conflicti561 – 5611N → S in AAA34924 (PubMed:6098824).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10029 Genomic DNA. Translation: AAA34924.1.
M22785 Genomic DNA. No translation available.
U00062 Genomic DNA. Translation: AAB68907.1.
BK006934 Genomic DNA. Translation: DAA06728.1.
PIRiS46738. RDBYC.
RefSeqiNP_011902.1. NM_001179167.1.

Genome annotation databases

EnsemblFungiiYHR037W; YHR037W; YHR037W.
GeneIDi856432.
KEGGisce:YHR037W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10029 Genomic DNA. Translation: AAA34924.1.
M22785 Genomic DNA. No translation available.
U00062 Genomic DNA. Translation: AAB68907.1.
BK006934 Genomic DNA. Translation: DAA06728.1.
PIRiS46738. RDBYC.
RefSeqiNP_011902.1. NM_001179167.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OE4X-ray2.17A/B23-575[»]
4OE6X-ray1.95A/B23-575[»]
ProteinModelPortaliP07275.
SMRiP07275. Positions 43-565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36468. 23 interactions.
IntActiP07275. 3 interactions.
MINTiMINT-640995.

Proteomic databases

MaxQBiP07275.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR037W; YHR037W; YHR037W.
GeneIDi856432.
KEGGisce:YHR037W.

Organism-specific databases

EuPathDBiFungiDB:YHR037W.
SGDiS000001079. PUT2.

Phylogenomic databases

GeneTreeiENSGT00560000077335.
HOGENOMiHOG000271511.
InParanoidiP07275.
KOiK00294.
OMAiTDYRYPF.
OrthoDBiEOG7BCNMF.

Enzyme and pathway databases

UniPathwayiUPA00261; UER00374.
BioCyciMetaCyc:MONOMER-646.
YEAST:YHR037W-MONOMER.
ReactomeiR-SCE-70688. Proline catabolism.

Miscellaneous databases

PROiP07275.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005931. P5CDH/ALDH4A1.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01236. D1pyr5carbox1. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of the nuclear PUT2 gene involved in the mitochondrial pathway for proline utilization in Saccharomyces cerevisiae."
    Krzywicki K.A., Brandriss M.C.
    Mol. Cell. Biol. 4:2837-2842(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "A regulatory region responsible for proline-specific induction of the yeast PUT2 gene is adjacent to its TATA box."
    Siddiqui A.H., Brandriss M.C.
    Mol. Cell. Biol. 8:4634-4641(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
  5. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
    Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
    Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPUT2_YEAST
AccessioniPrimary (citable) accession number: P07275
Secondary accession number(s): D3DKY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 17200 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.