5-aminolevulinate synthase, mitochondrial precursor - Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast)

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P78698 (HEM1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. History...

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

Documents (2) |

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
Ordered Locus Names:	KLLA0C15059g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

Taxonomic lineage

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

Protein attributes

Sequence length	570 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.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
Subcellular location	Mitochondrion matrix.
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
Gene Ontology (GO)
Biological_process	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 electronic annotation. Source: EC 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

? – 570

5-aminolevulinate synthase, mitochondrial

PRO_0000001241

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

Experimental info

Sequence conflict

1

A → R in CAA63497. Ref.1

Sequence conflict

1

T → S in CAA63497. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P78698 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: CD9151C4A529AA89
Show »

570

62,139

        10         20         30         40         50         60 
MESVIRSSAK ICPFMHSATG SMQSVKALKN ANLPAIAQQC PFMGKAMEQR RGYASSASGA 

        70         80         90        100        110        120 
SAAAAATATA STSASNSNSS VEASASADVV DHATKEASFD YQGLFDSDLA KKRMDKSYRF 

       130        140        150        160        170        180 
FNNINRLAKE FPMAHRKLED DKVTVWCSND YLALSKNQEV IEVMKKTLDK YGAGAGGTRN 

       190        200        210        220        230        240 
IAGHNKHALQ LEAELATLHK KEGALVFSSC FVANDAVISL LGQKIKDLVI FSDELNHASM 

       250        260        270        280        290        300 
IVGIKHASTK KHIFKHNNLD QLEELLAMYP KSTPKLIAFE SVYSMSGSVA DIDKICDLAE 

       310        320        330        340        350        360 
KYGALTFLDE VHAVGLYGPH GAGVAEHCNF DAHRKAGIAS PEFRTVMDRV DMITGTLGKS 

       370        380        390        400        410        420 
FGTVGGYVAG SLQLIDWVRS YAPGFIFTTT LPPAVMAGAA EAIRYQRSHL DLRQDQQRHT 

       430        440        450        460        470        480 
TYVKDGLADL GIPVMPNPSH IVPVLVGNPH LAKQASDILM DKHRIYVQAI NFPTVARGTE 

       490        500        510        520        530        540 
RLRITPTPGH TNDLSDILMD ALEDVWSTLQ LPRVRDWEAQ GGLLGVGDPN HVPQPNLWTK 

       550        560        570 
DQLTLTNNDL HPNVKQPIIE QLEVSSGIRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the KlHEM1 gene in Kluyveromyces lactis." Gonzales-Dominguez M., Mendez-Carro C., Cerdan M.E. Yeast 13:961-971(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X92944 Genomic DNA. Translation: CAA63497.1. CR382123 Genomic DNA. Translation: CAH01726.1.
RefSeq	XP_452875.1. XM_452875.1.
3D structure databases
ProteinModelPortal	P78698.
ModBase	Search...
Protein-protein interaction databases
STRING	28985.P78698.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2892616.
KEGG	kla:KLLA0C15059g.
Phylogenomic databases
eggNOG	COG0156.
HOGENOM	HOG000221020.
KO	K00643.
OMA	GAYPNAR.
OrthoDB	EOG412QDQ.
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_KLULA

Accession

Primary (citable) accession number: P78698
Secondary accession number(s): Q6CT64

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 27, 2004
Last modified:	May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

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