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P09950 (HEM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-aminolevulinate synthase, mitochondrial

EC=2.3.1.37
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene names
Name:HEM1
Synonyms:CYD1
Ordered Locus Names:YDR232W
ORF Names:YD9934.16
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.

Cofactor

Pyridoxal phosphate.

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion matrix Ref.6.

Miscellaneous

Present with 22600 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 5485-aminolevulinate synthase, mitochondrialPRO_0000001245

Regions

Compositional bias26 – 6237Ala-rich
Compositional bias54 – 629Poly-Ala

Sites

Active site3371 By similarity
Binding site911Substrate By similarity
Binding site2041Substrate By similarity
Binding site2231Substrate By similarity
Binding site2561Pyridoxal phosphate By similarity
Binding site2841Pyridoxal phosphate By similarity
Binding site3341Pyridoxal phosphate By similarity
Binding site3661Pyridoxal phosphate By similarity
Binding site3671Pyridoxal phosphate By similarity
Binding site4521Substrate By similarity

Amino acid modifications

Modified residue3371N6-(pyridoxal phosphate)lysine Probable

Experimental info

Sequence conflict1811S → P in AAU09697. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P09950 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: FAAEDBAFCEDBE429

FASTA54859,362
        10         20         30         40         50         60 
MQRSIFARFG NSSAAVSTLN RLSTTAAPHA KNGYATATGA GAAAATATAS STHAAAAAAA 

        70         80         90        100        110        120 
AANHSTQESG FDYEGLIDSE LQKKRLDKSY RYFNNINRLA KEFPLAHRQR EADKVTVWCS 

       130        140        150        160        170        180 
NDYLALSKHP EVLDAMHKTI DKYGCGAGGT RNIAGHNIPT LNLEAELATL HKKEGALVFS 

       190        200        210        220        230        240 
SCYVANDAVL SLLGQKMKDL VIFSDELNHA SMIVGIKHAN VKKHIFKHND LNELEQLLQS 

       250        260        270        280        290        300 
YPKSVPKLIA FESVYSMAGS VADIEKICDL ADKYGALTFL DEVHAVGLYG PHGAGVAEHC 

       310        320        330        340        350        360 
DFESHRASGI ATPKTNDKGG AKTVMDRVDM ITGTLGKSFG SVGGYVAASR KLIDWFRSFA 

       370        380        390        400        410        420 
PGFIFTTTLP PSVMAGATAA IRYQRCHIDL RTSQQKHTMY VKKAFHELGI PVIPNPSHIV 

       430        440        450        460        470        480 
PVLIGNADLA KQASDILINK HQIYVQAINF PTVARGTERL RITPTPGHTN DLSDILINAV 

       490        500        510        520        530        540 
DDVFNELQLP RVRDWESQGG LLGVGESGFV EESNLWTSSQ LSLTNDDLNP NVRDPIVKQL 


EVSSGIKQ 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of the HEM1 gene and evidence for a precursor form of the mitochondrial 5-aminolevulinate synthase in Saccharomyces cerevisiae."
Urban-Grimal D., Volland C., Garnier T., Dehoux P., Labbe-Bois R.
Eur. J. Biochem. 156:511-519(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Constitutive expression of the yeast HEM1 gene is actually a composite of activation and repression."
Keng T., Guarente L.
Proc. Natl. Acad. Sci. U.S.A. 84:9113-9117(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2.
[6]"The nine amino-terminal residues of delta-aminolevulinate synthase direct beta-galactosidase into the mitochondrial matrix."
Keng T., Alani E., Guarente L.
Mol. Cell. Biol. 6:355-364(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75, SUBCELLULAR LOCATION.
[7]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26329 Genomic DNA. Translation: AAA34668.1.
Z48612 Genomic DNA. Translation: CAA88511.1.
AY723780 Genomic DNA. Translation: AAU09697.1.
J03556 Genomic DNA. No translation available.
BK006938 Genomic DNA. Translation: DAA12073.1.
PIRSYBYAL. A24870.
RefSeqNP_010518.1. NM_001180540.1.

3D structure databases

ProteinModelPortalP09950.
SMRP09950. Positions 72-481.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32283. 39 interactions.
IntActP09950. 4 interactions.
MINTMINT-4481528.
STRING4932.YDR232W.

Proteomic databases

MaxQBP09950.
PaxDbP09950.
PeptideAtlasP09950.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR232W; YDR232W; YDR232W.
GeneID851818.
KEGGsce:YDR232W.

Organism-specific databases

CYGDYDR232w.
SGDS000002640. HEM1.

Phylogenomic databases

eggNOGCOG0156.
GeneTreeENSGT00530000063111.
HOGENOMHOG000221020.
KOK00643.
OMAKLAQYPK.
OrthoDBEOG7HHX1P.

Enzyme and pathway databases

BioCycYEAST:YDR232W-MONOMER.
UniPathwayUPA00251; UER00375.

Gene expression databases

GenevestigatorP09950.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01821. 5aminolev_synth. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969683.
PROP09950.

Entry information

Entry nameHEM1_YEAST
AccessionPrimary (citable) accession number: P09950
Secondary accession number(s): D6VSL3, E9P946
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 14, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways