Reviewed, UniProtKB/Swiss-Prot Q75DX7 (HEM1_ASHGO)

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 synthase

Gene names

Name:	HEM1
Ordered Locus Names:	ABL104C

Organism

Ashbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]

Taxonomic identifier

33169 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	556 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	? – 556		5-aminolevulinate synthase, mitochondrial		PRO_0000001236
Amino acid modifications
	Modified residue	345	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q75DX7-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: DABDD7E6FEB4E764	FASTA	556	61,222
	10 20 30 40 50 60 MDSLARQSAK ICPFVSRVTS SMQQVQVLHK TNMSAMAQQC PVMRRAMAAR GYVTASPPAG 70 80 90 100 110 120 AAAADVGEAR PITPVLERGT QERTFDYDGL FETELQKKRL DSSYRFFNNI NRLAKEYPMA 130 140 150 160 170 180 HRLEEEDKVT VWCSNDYLTY SRNEKVMETM KRTIDKYGAG AGGTRNIAGH NRHAMRLEAE 190 200 210 220 230 240 LAALHKKEGA LVFSSCFVAN DAVLSLLGQK MPNMVIFSDE MNHASMIMGI KHANVQKHIF 250 260 270 280 290 300 RHNDLQHLEE LLAMYPKSQP KLIAFESVYS MSGSVADIRK ICDLAEKYGA LTFLDEVHSV 310 320 330 340 350 360 GLYGPHGAGV AEHLDFEAHR KAGLASPAQT TVLDRVDMIT ATLGKSFGSV GGYLAASEKL 370 380 390 400 410 420 VDFVRSYAPG FIFTSSLPPA VMAGSAAAVF DQRSSLHLRQ LQQKHTSYVK TGLGDLGIPV 430 440 450 460 470 480 QPNPSHIVPV LVGNPDLAKR ASDILMEKHR IYVQAINFPT VPRGTERLRI TPTPGHTNDL 490 500 510 520 530 540 SDVLLDAMDD VWKTLQLPRV SDWAAHGGLL GVGEPDYVPE ANLWTEEQMS LTNDDLHPSV 550 FSPVEKFLEV SSGIKA

References

[1]

"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed: 15001715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016815 Genomic DNA. Translation: AAS50667.1.
RefSeq	NP_982843.1.
3D structure databases
SMR	Q75DX7. Positions 86-492.
ModBase	Search...
Protein-protein interaction databases
STRING	Q75DX7.
Genome annotation databases
GeneID	4618923.
GenomeReviews	Gene locus ABL104C in contig AE016815_GR.
KEGG	ago:AGOS_ABL104C.
NMPDR	fig|33169.1.peg.488.
Organism-specific databases
AGD	ABL104C.
Phylogenomic databases
eggNOG	fuNOG07159.
HOGENOM	HBG649839.
OMA	HLKESNE.
OrthoDB	EOG9CVHQ2.
Enzyme and pathway databases
BRENDA	2.3.1.37. 279361.
Family and domain databases
InterPro	IPR010961. 4pyrrol_synth_NH2levulA_synth. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase_major_dom. 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_ASHGO

Accession

Primary (citable) accession number: Q75DX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	July 5, 2004
Last modified:	February 9, 2010
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)