Reviewed, UniProtKB/Swiss-Prot Q9XT75 (HEM0_DELLE)

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:	ALS2

Organism

Delphinapterus leucas (Beluga whale)

Taxonomic identifier

9749 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Cetacea › Odontoceti › Monodontidae › Delphinapterus

Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion matrix By similarity.
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.

Ontologies

Keywords
Biological process	Heme biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	erythrocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB heme biosynthetic process 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?44	44	Mitochondrion Potential
	Chain	?45 – 582	538	5-aminolevulinate synthase, erythroid-specific, mitochondrial		PRO_0000001222
Amino acid modifications
	Modified residue	386	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9XT75-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 7C15EBF6C154C34D	FASTA	582	64,555
	10 20 30 40 50 60 MLLQRCPVLI RSPTAILGKM IKTHQFLIGI GRCPILATQG TTCSQIHLKA TKAGGDSPSW 70 80 90 100 110 120 AKSHCPFMLL ELQDGKSKIV QKAAPEVQED VKTFKTDLPI SLASTSLRKP FFSPQEPEKN 130 140 150 160 170 180 SEKVTHLIQN NMAGNHVFGY DQFFRNKIME KKQDHTYRVF KTVNRWADAY PFAEHFFEAS 190 200 210 220 230 240 VASKDVSVWC SNDYLGMSRH PRVLQATQET LQRHGAGAGG TRNISGTSRF HVELEQELAE 250 260 270 280 290 300 LHQKDSALLF SSCFVANDST LFTLAKILPG CEIYSDAGNH ASMIQGIRNS GAAKFVFRHN 310 320 330 340 350 360 DPDHLKKLLK KSNPETPKIV AFETVHSMDG AICPLEELCD VAHQYGALTF VDEVHAVGLY 370 380 390 400 410 420 GSRGAGIGER DGIMHKIDII SGTLGKAFGC VGGYIASTRD LVDMVRSYAA GFIFTTSLPP 430 440 450 460 470 480 MVLSGALESV RLLKGEEGQA LRRAHQRNVK HMRQLLMDRG LPVIPCPSHI IPIRVGDAAL 490 500 510 520 530 540 NSRICDLLLS KHGIYVQAIN YPTVPRGEEL LRLAPSPHHS PQMMEDFVEK LLAAWTEVGL 550 560 570 580 PLQDVSIAAC NFCRRPVHFE LMSEWERSYF GNMGPQYVTT YA

References

[1]

"Comparison of the beluga whale (Delphinapterus leucas) expressed genes for 5-aminolevulinate synthase with those in other vertebrates." Kreiling J.A., Duncan R., Faggart M.A., Cornell N.W. Comp. Biochem. Physiol. 123B:163-174(1999) [PubMed: 10425720] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF086786 mRNA. Translation: AAD41464.1.
3D structure databases
HSSP	HSSP built from PDB template 1H7D based on UniProtKB P08680.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q9XT75.
Enzyme and pathway databases
BRENDA	2.3.1.37. 191613.
Family and domain databases
InterPro	IPR010961. 4pyrrol_synth_NH2levulA_synth. IPR015118. 5aminolev_synth_preseq. 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. PF09029. Preseq_ALAS. 1 hit. [Graphical view]
TIGRFAMs	TIGR01821. 5aminolev_synth. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM0_DELLE

Accession

Primary (citable) accession number: Q9XT75

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	November 1, 1999
Last modified:	September 22, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)