5-aminolevulinate synthase, mitochondrial precursor - Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

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O94069 (HEM1_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 92. History...

Clusters with 100%, 90%, 50% identity |

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Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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
ORF Names:	Ca49C4.15, CaO19.2601

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida ›

Protein attributes

Sequence length	564 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO₂.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Biological process	Heme biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	heme biosynthetic process Inferred from mutant phenotype PubMed 15893902. Source: CGD protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	5-aminolevulinate synthase activity Inferred from mutant phenotype PubMed 15893902. Source: CGD pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion

Chain

? – 564

5-aminolevulinate synthase, mitochondrial

PRO_0000001237

Sites

Active site

1

By similarity

Binding site

1

Substrate By similarity

Binding site

1

Substrate By similarity

Binding site

1

Substrate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Substrate By similarity

Amino acid modifications

Modified residue

1

N6-(pyridoxal phosphate)lysine Probable

Sequences

Sequence

Length

Mass (Da)

Tools

O94069 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C984334068F40487
Show »

564

61,395

        10         20         30         40         50         60 
MESITKVSMS VCPFVRSTST QALRQLSQTS GALANQARQC PIAGNAIRAK EISIRSYSSA 

        70         80         90        100        110        120 
TKPVRATAAT PSTPEATFNV SSSFELGSKE TAFDYNGYLG NELEKKRSDK SYRYFNNINR 

       130        140        150        160        170        180 
LANEFPKAHR TQEEDKVTVW CSNDYLGMGK NENTLKEMKR VLDKYGSGAG GTRNIAGHNS 

       190        200        210        220        230        240 
HAIKLESELA ALHKHDAALV FSSCFVANDA VLSLLGQKIK DLVIFSDELN HASMIQGIRN 

       250        260        270        280        290        300 
SRARKHIFKH NNLADLESKL AQYPKSTPKL IAFESVYSMC GSIAPIEAIC DLAEKYGALT 

       310        320        330        340        350        360 
FLDEVHAVGM YGPHGAGVAE HLNFEAHLKS GIERPEITTV MSRVDMVTGT LGKAYGVVGG 

       370        380        390        400        410        420 
YITGKTNLID WFRSYAPGFI FTTSLPPAIM AGCSASIRYQ RATLKDRIAQ QKNTRLVKNN 

       430        440        450        460        470        480 
LNELGIPVIP NPSHIVPVLV GNAADAKRAS DLLLNKHDIY VQAINFPTVP IGEERLRITP 

       490        500        510        520        530        540 
TPGHGPELSK QLVEAVDSVF TELNLNRIND WKKLGGLVGV GVEGAAKVEH IWTEEQLALT 

       550        560 
DADLNPNVVN PAISPLDVSS GIST

References

[1]	"Candida albicans strain 1161 genome pilot sequencing project." Murphy L., Harris D., Barrell B.G., Rajandream M.A. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1161.
[2]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL033503 Genomic DNA. Translation: CAA22025.1. AACQ01000044 Genomic DNA. Translation: EAK99337.1.
PIR	T18251.
RefSeq	XP_718266.1. XM_713173.1.
3D structure databases
ProteinModelPortal	O94069.
ModBase	Search...
Protein-protein interaction databases
STRING	5476.CAL0003351.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3640149.
KEGG	cal:CaO19.2601.
Organism-specific databases
CGD	CAL0003351. HEM1.
Phylogenomic databases
eggNOG	COG0156.
KO	K00643.
Enzyme and pathway databases
UniPathway	UPA00251; UER00375.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR010961. 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]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01821. 5aminolev_synth. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_CANAL

Accession

Primary (citable) accession number: O94069
Secondary accession number(s): Q5A965

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents