5-aminolevulinate synthase, mitochondrial precursor - Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast)

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Q6BX71 (HEM1_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. 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:	DEHA2B05478g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces ›

Protein attributes

Sequence length	575 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
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 Potential

Chain

? – 575

5-aminolevulinate synthase, mitochondrial

PRO_0000001239

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 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6BX71 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 05107F73EB488A2C
Show »

575

62,652

        10         20         30         40         50         60 
MESITRVSMS VCPFVKSSSA QALRQLSKNS ALTSQARQCP FMGAALNAKE STRSYSSATK 

        70         80         90        100        110        120 
PVRATASSLA SNPPSTMQSK YSFKAEELVG NKDAINLESK ENTFDFKGYL NSELSKKRTD 

       130        140        150        160        170        180 
KSYRFFNNIN RLANEFPKAH RSEENDKVTV WCSNDYLGMG KNENTINEMK RVLTKYGSGA 

       190        200        210        220        230        240 
GGTRNIAGHN IHALKLESEL AALHKHEAAL VFSSCFVAND AVLSLFGQKI KDLVIFSDEL 

       250        260        270        280        290        300 
NHASMIQGIR NSRAKKQVFK HNDLADLEEK LAQYPKSTPK LIAFESVYSM CGSIAPIEAI 

       310        320        330        340        350        360 
CDLAEKYGAL TFLDEVHAVG MYGPHGAGVA EHLDFDAHLK SGIASPQTQT VMNRVDMVTG 

       370        380        390        400        410        420 
TLGKAYGTVG GYITGKANLI DWFRSFAPGF IFTTTLPPSI MAGSSASIRY QRSTLQDRIA 

       430        440        450        460        470        480 
QQTNTRYVKN NLTDIGIPVI PNPSHIVPVL VGNALDAKKA SDLLLDKYNI YVQAINFPTV 

       490        500        510        520        530        540 
PIGQERLRIT PTPGHGPELS NQLIGALDSV FNELSLSRIG DWEGKGGLCG VGEPDIEPIE 

       550        560        570 
HIWTSEQLAL TDADINPNVI DPVIQPIGVS SGVRD

References

[1]

"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.

expand/collapse author list

Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382134 Genomic DNA. Translation: CAG85193.1.
RefSeq	XP_457198.1. XM_457198.1.
3D structure databases
ProteinModelPortal	Q6BX71.
ModBase	Search...
Protein-protein interaction databases
STRING	4959.Q6BX71.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2913002.
KEGG	dha:DEHA2B05478g.
Phylogenomic databases
eggNOG	COG0156.
KO	K00643.
OMA	HANKQIV.
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_DEBHA

Accession

Primary (citable) accession number: Q6BX71

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 67 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

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