Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Sitei212Transition state stabilizerBy similarity1
Active sitei317Proton acceptorPROSITE-ProRule annotation1
Active sitei351NucleophilePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi297 – 302NADBy similarity6

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:YHR037W-MONOMER.
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)DescriptionActionsGraphical viewLength
ChainiPRO_0000007177? – 575Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

MaxQBiP07275.
PRIDEiP07275.

Expressioni

Inductioni

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

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1575
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi44 – 56Combined sources13
Beta strandi59 – 61Combined sources3
Beta strandi63 – 65Combined sources3
Beta strandi68 – 70Combined sources3
Turni73 – 75Combined sources3
Beta strandi78 – 83Combined sources6
Beta strandi86 – 95Combined sources10
Helixi99 – 117Combined sources19
Helixi121 – 136Combined sources16
Turni137 – 139Combined sources3
Helixi140 – 151Combined sources12
Helixi155 – 162Combined sources8
Helixi164 – 180Combined sources17
Beta strandi193 – 200Combined sources8
Beta strandi202 – 208Combined sources7
Helixi214 – 226Combined sources13
Beta strandi231 – 234Combined sources4
Helixi237 – 239Combined sources3
Helixi240 – 252Combined sources13
Beta strandi259 – 262Combined sources4
Helixi267 – 274Combined sources8
Beta strandi280 – 287Combined sources8
Helixi289 – 305Combined sources17
Beta strandi313 – 317Combined sources5
Beta strandi322 – 326Combined sources5
Helixi332 – 344Combined sources13
Helixi345 – 348Combined sources4
Beta strandi354 – 360Combined sources7
Helixi361 – 377Combined sources17
Helixi405 – 418Combined sources14
Beta strandi424 – 428Combined sources5
Beta strandi435 – 437Combined sources3
Beta strandi443 – 449Combined sources7
Helixi453 – 455Combined sources3
Beta strandi461 – 469Combined sources9
Helixi471 – 473Combined sources3
Helixi474 – 483Combined sources10
Beta strandi489 – 494Combined sources6
Helixi498 – 507Combined sources10
Turni508 – 510Combined sources3
Beta strandi513 – 519Combined sources7
Helixi548 – 552Combined sources5
Beta strandi553 – 560Combined sources8

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00560000077335.
HOGENOMiHOG000271511.
InParanoidiP07275.
KOiK00294.
OMAiTDYRYPF.
OrthoDBiEOG092C19IG.

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)DescriptionActionsGraphical viewLength
Sequence conflicti187 – 188ES → SR in AAA34924 (PubMed:6098824).Curated2
Sequence conflicti264P → L in AAA34924 (PubMed:6098824).Curated1
Sequence conflicti541D → G in AAA34924 (PubMed:6098824).Curated1
Sequence conflicti561N → S in AAA34924 (PubMed:6098824).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OE4X-ray2.17A/B23-575[»]
4OE6X-ray1.95A/B23-575[»]
ProteinModelPortaliP07275.
SMRiP07275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP07275.
PRIDEiP07275.

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.
OrthoDBiEOG092C19IG.

Enzyme and pathway databases

UniPathwayiUPA00261; UER00374.
BioCyciMetaCyc:YHR037W-MONOMER.
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...

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: November 2, 2016
This is version 166 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.