Reviewed, UniProtKB/Swiss-Prot P07275 (PUT2_YEAST)

Names and origin

Protein names

Recommended name:
    Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
      Short name=P5C dehydrogenase
    EC=1.5.1.12

Gene names

Name:	PUT2
Ordered Locus Names:	YHR037W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	(S)-1-pyrroline-5-carboxylate + NAD(P)+ + 2 H2O = L-glutamate + NAD(P)H.
Pathway	Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
Subcellular location	Mitochondrion inner membrane. Ref.4
Induction	By proline and is regulated by a common control element encoded by the PUT3 gene.
Miscellaneous	Present with 17200 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Biological process	Proline metabolism
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamate biosynthetic process Traceable author statement. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW proline biosynthetic process Inferred from electronic annotation. Source: InterPro proline catabolic process to glutamate Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial matrix Inferred from electronic annotation. Source: InterPro
Molecular function	1-pyrroline-5-carboxylate dehydrogenase activity Inferred from mutant phenotype. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-14303,EBI-14303
SSA2	P10592	1	EBI-14303,EBI-8603

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 575		Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial		PRO_0000007177
Regions
	Nucleotide binding	297 – 302	6	NAD By similarity
Sites
	Active site	317	1	Proton acceptor By similarity
	Active site	351	1	Nucleophile By similarity
	Site	212	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	187 – 188	2	ES → SR in AAA34924. Ref.1
	Sequence conflict	264	1	P → L in AAA34924. Ref.1
	Sequence conflict	541	1	D → G in AAA34924. Ref.1
	Sequence conflict	561	1	N → S in AAA34924. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P07275-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 5A610D67985291B0	FASTA	575	64,435
	10 20 30 40 50 60 MLSARCLKSI YFKRSFSQLG HIKPPKHIRN EPVKPFRNID LKDWDLLRAS LMKFKSSSLE 70 80 90 100 110 120 VPLVINGERI YDNNERALFP QTNPANHQQV LANVTQATEK DVMNAVKAAK DAKKDWYNLP 130 140 150 160 170 180 FYDRSAIFLK AADLISTKYR YDMLAATMLG QGKNVYQAEI DCITELSDFF RYYVKYASDL 190 200 210 220 230 240 YAQQPVESAD GTWNKAEYRP LEGFVYAVSP FNFTAIAANL IGAPALMGNT VVWKPSQTAA 250 260 270 280 290 300 LSNYLLMTVL EEAGLPKGVI NFIPGDPVQV TDQVLADKDF GALHFTGSTN VFKSLYGKIQ 310 320 330 340 350 360 SGVVEGKYRD YPRIIGETGG KNFHLVHPSA NISHAVLSTI RGTFEFQGQK CSAASRLYLP 370 380 390 400 410 420 ESKSEEFLSD MFGILQSQNV VPMNTSASPI SGGNLRGFMG PVIHEQSFDK LVKVIEDAKK 430 440 450 460 470 480 DPELEILYGG QYDKSQGWFV GPTVIKAKRP DHPYMSTEFF GPILTVYEYP DTEFNEICDI 490 500 510 520 530 540 IDNTSQYALT GAIFAKDRKA IEYADEKLKF SAGNFYINDK CTGAVVSQQW FGGARMSGTD 550 560 570 DKAGGPNILS RFVSIRNTKE NFYELTDFKY PSNYE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 6098824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 3062363] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
[4]	"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: 11502169] [Abstract] Cited for: SUBCELLULAR LOCATION.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M10029 Genomic DNA. Translation: AAA34924.1. M22785 Genomic DNA. No translation available. U00062 Genomic DNA. Translation: AAB68907.1.
PIR	RDBYC. S46738.
RefSeq	NP_011902.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P07275. 3 interactions.
STRING	P07275.
Proteomic databases
PeptideAtlas	P07275.
Genome annotation databases
Ensembl	YHR037W; YHR037W; YHR037W; Saccharomyces cerevisiae. [Genome view]
GeneID	856432.
GenomeReviews	Gene locus YHR037W in contig U00093_GR.
KEGG	sce:YHR037W.
NMPDR	fig|4932.3.peg.3051.
Organism-specific databases
CYGD	YHR037w.
SGD	S000001079. PUT2.
Phylogenomic databases
HOGENOM	P07275.
OMA	RYAAGNY.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-646.
BRENDA	1.5.1.12. 250.
Gene expression databases
ArrayExpress	P07275.
Genevestigator	P07275.
GermOnline	YHR037W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. IPR005931. d-1-pyrroline-5-COlate_DH-1. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01236. D1pyr5carbox1. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	982024.

Entry information

Entry name

PUT2_YEAST

Accession

Primary (citable) accession number: P07275

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	February 1, 1995
Last modified:	November 3, 2009
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)