Reviewed, UniProtKB/Swiss-Prot Q6BX71 (HEM1_DEBHA)

Names and origin

Protein names

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

Gene names

Name:	HEM1
Ordered Locus Names:	DEHA2B05478g

Organism

Debaryomyces hansenii (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

4959 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › 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	heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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 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 – ?		Mitochondrion Potential
	Chain	? – 575		5-aminolevulinate synthase, mitochondrial		PRO_0000001239
Amino acid modifications
	Modified residue	364	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BX71-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 05107F73EB488A2C	FASTA	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. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382134 Genomic DNA. Translation: CAG85193.1.
RefSeq	XP_457198.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6BX71.
Genome annotation databases
GeneID	2913002.
GenomeReviews	Gene locus DEHA2B05478g in contig CR382134_GR.
KEGG	dha:DEHA0B05357g.
Phylogenomic databases
HOGENOM	Q6BX71.
OMA	FSPIKDI.
Enzyme and pathway databases
BRENDA	2.3.1.37. 74267.
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...

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:	November 3, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)