5-aminolevulinate synthase, erythroid-specific, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot Q9YHT4 (HEM0_DANRE)

Last modified November 3, 2009. Version 70. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    5-aminolevulinate synthase, erythroid-specific, mitochondrial
    EC=2.3.1.37
Alternative name(s):
    5-aminolevulinic acid synthase
    Delta-aminolevulinate synthase
    Delta-ALA synthetase
      Short name=ALAS-E

Gene names

Name:	alas2
Synonyms:	alas-e

Organism

Danio rerio (Zebrafish) (Brachydanio rerio)

Taxonomic identifier

7955 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

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Protein attributes

Sequence length	583 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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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.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion matrix.
Miscellaneous	There are two delta-ALA synthetase in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues.
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

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Ontologies

Keywords
Biological process	Heme biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	embryonic hemopoiesis Ref.1 Inferred from mutant phenotype. Source: ZFIN erythrocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB heme biosynthetic process Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB hemoglobin biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB response to hypoxia Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrial inner membrane Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	5-aminolevulinate synthase activity Inferred from sequence or structural similarity. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion Potential

Chain

? – 583

5-aminolevulinate synthase, erythroid-specific, mitochondrial

PRO_0000001227

Amino acid modifications

Modified residue

386

N6-(pyridoxal phosphate)lysine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9YHT4-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 9C542B4C75299ABD
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FASTA

583

63,909

        10         20         30         40         50         60 
MSAFLHHCPF LKSSPGPSAR KVATYLNLAD RCPIIVRQIS AKAAQSSEQN GLLPHKEPKR 

        70         80         90        100        110        120 
QLATTATQVA VSMSQSCPFV SSKIGLVKAS PQVQEDVQPN LENQDTSGLI SSLFSGLQSH 

       130        140        150        160        170        180 
QSTGPTHLLQ DNFNRPTFSY DEFFTQKIVE KKKDHTYRIF KTVNRFAEVF PFAEDYSIAG 

       190        200        210        220        230        240 
RLGSQVSVWC SNDYLGMSRH PRVVKAIGDA LKKHGAGAGG TRNISGTSNY HVALENELAR 

       250        260        270        280        290        300 
LHQKDGALVF SSCFVANDST LFTLAKMLPG CEIYSDMGNH ASMIQGIRNS GAKRFIFRHN 

       310        320        330        340        350        360 
DASHLEELLS RSDPLTPKIV AFETVHSMDG AICPLEELCD VAHKYGALTF VDEVHAVGLY 

       370        380        390        400        410        420 
GAHGAGVGER DNVMHKIDIV SGTLGKAFGC VGGYIASTAA LVDTVRSFAA GFIFTTSLPP 

       430        440        450        460        470        480 
MVLAGALESV RVLKSDEGQA LRRAHQRNVK HMRQLLLDAG LPVVNCPSHI IPIRVGNAAK 

       490        500        510        520        530        540 
NSEVCDILLE KHNIYVQAIN YPTVPRGEEL LRLAPSPFHN PIMMNYFAEK LLDVWQEVGL 

       550        560        570        580 
PLNGPAQASC TFCDRPLHFD LMSEWEKSYF GNMEPRYITV AAQ

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Positional cloning of the zebrafish sauternes gene: a model for congenital sideroblastic anaemia." Brownlie A., Donovan A., Pratt S.J., Paw B.H., Oates A.C., Brugnara C., Witkowska H.E., Sassa S., Zon L.I. Nat. Genet. 20:244-250(1998) [PubMed: 9806542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	NIH - Zebrafish Gene Collection (ZGC) project Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	AF095747 mRNA. Translation: AAC72835.1. BC056338 mRNA. Translation: AAH56338.1. BC067149 mRNA. Translation: AAH67149.1. Different initiation.
IPI	IPI00490337.
RefSeq	NP_571757.1.
UniGene	Dr.8180
3D structure databases
HSSP	HSSP built from PDB template 1FC4 based on UniProtKB P07912.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9YHT4.
Genome annotation databases
Ensembl	ENSDART00000056420; ENSDARP00000056419; ENSDARG00000038643; Danio rerio. [Genome view]
GeneID	64607.
KEGG	dre:64607.
Organism-specific databases
CTD	64607.
ZFIN	ZDB-GENE-001229-1. alas2.
Phylogenomic databases
HOGENOM	Q9YHT4.
HOVERGEN	Q9YHT4.
OMA	FSPIKDI.
Enzyme and pathway databases
BRENDA	2.3.1.37. 96826.
Gene expression databases
ArrayExpress	Q9YHT4.
Bgee	Q9YHT4.
Family and domain databases
InterPro	IPR010961. 4pyrrol_synth_NH2levulA_synth. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR01821. 5aminolev_synth. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

HEM0_DANRE

Accession

Primary (citable) accession number: Q9YHT4
Secondary accession number(s): Q6NXC5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Zebrafish annotation project

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents