ALD5/YER073W Protein Information

Standard Name	Ald5p
Systematic Name	Yer073wp
ORF Classification	Verified
Description	Mitochondrial aldehyde dehydrogenase, involved in regulation or biosynthesis of electron transport chain components and acetate formation; activated by K+; utilizes NADP+ as the preferred coenzyme; constitutively expressed (1, 2, 3)
Name Description	ALdehyde Dehydrogenase

Experimental Data
Molecules/cell	23300 4

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	520
Molecular Weight (Da)	56,693
Isoelectric Point (pI)	8.32

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Ald5p (InterPro)
Physical Interactions	There are 9 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000158ECC0 \| P40047 MIPS: YER073W NCBI: 1336078 \| 1706378 \| 330443526 \| 341940622 \| 603310 \| NP_010996.2 GenBank/EMBL/DDBJ: DAA07732.2 \| U18814 \| U56605
External Classifications	EC: 1.2.1.3 [Aldehyde dehydrogenase (NAD(+))] EC: 1.2.1.4 [Aldehyde dehydrogenase (NADP(+))] EC: 1.2.1.5 [Aldehyde dehydrogenase (NAD(P)(+))]

Amino Acid Sequence (or in FASTA format)
1 MLSRTRAAAP NSRIFTRSLL RLYSQAPLRV PITLPNGFTY EQPTGLFING 51 EFVASKQKKT FDVINPSNEE KITTVYKAME DDVDEAVAAA KKAFETKWSI 101 VEPEVRAKAL FNLADLVEKH QETLAAIESM DNGKSLFCAR GDVALVSKYL 151 RSCGGWADKI YGNVIDTGKN HFTYSIKEPL GVCGQIIPWN FPLLMWSWKI 201 GPALATGNTV VLKPAETTPL SALFASQLCQ EAGIPAGVVN ILPGSGRVVG 251 ERLSAHPDVK KIAFTGSTAT GRHIMKVAAD TVKKVTLELG GKSPNIVFAD 301 ADLDKAVKNI AFGIFYNSGE VCCAGSRIYI QDTVYEEVLQ KLKDYTESLK 351 VGDPFDEEVF QGAQTSDKQL HKILDYVDVA KSEGARLVTG GARHGSKGYF 401 VKPTVFADVK EDMRIVKEEV FGPIVTVSKF STVDEVIAMA NDSQYGLAAG 451 IHTNDINKAV DVSKRVKAGT VWINTYNNFH QNVPFGGFGQ SGIGREMGEA 501 ALSNYTQTKS VRIAIDKPIR *

Amino Acid Sequence (or in FASTA format)

       1  MLSRTRAAAP NSRIFTRSLL RLYSQAPLRV PITLPNGFTY EQPTGLFING
      51  EFVASKQKKT FDVINPSNEE KITTVYKAME DDVDEAVAAA KKAFETKWSI
     101  VEPEVRAKAL FNLADLVEKH QETLAAIESM DNGKSLFCAR GDVALVSKYL
     151  RSCGGWADKI YGNVIDTGKN HFTYSIKEPL GVCGQIIPWN FPLLMWSWKI
     201  GPALATGNTV VLKPAETTPL SALFASQLCQ EAGIPAGVVN ILPGSGRVVG
     251  ERLSAHPDVK KIAFTGSTAT GRHIMKVAAD TVKKVTLELG GKSPNIVFAD
     301  ADLDKAVKNI AFGIFYNSGE VCCAGSRIYI QDTVYEEVLQ KLKDYTESLK
     351  VGDPFDEEVF QGAQTSDKQL HKILDYVDVA KSEGARLVTG GARHGSKGYF
     401  VKPTVFADVK EDMRIVKEEV FGPIVTVSKF STVDEVIAMA NDSQYGLAAG
     451  IHTNDINKAV DVSKRVKAGT VWINTYNNFH QNVPFGGFGQ SGIGREMGEA
     501  ALSNYTQTKS VRIAIDKPIR *

external links for Ald5p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Candida (CGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA

References cited on this page View Complete Literature Guide for Ald5p

1)	Navarro-Avino JP, et al. (1999) A proposal for nomenclature of aldehyde dehydrogenases in Saccharomyces cerevisiae and characterization of the stress-inducible ALD2 and ALD3 genes. Yeast 15(10A):829-42
2)	Kurita O and Nishida Y (1999) Involvement of mitochondrial aldehyde dehydrogenase ALD5 in maintenance of the mitochondrial electron transport chain in Saccharomyces cerevisiae. FEMS Microbiol Lett 181(2):281-7
3)	Saint-Prix F, et al. (2004) Functional analysis of the ALD gene family of Saccharomyces cerevisiae during anaerobic growth on glucose: the NADP+-dependent Ald6p and Ald5p isoforms play a major role in acetate formation. Microbiology 150(Pt 7):2209-20
4)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41