Reviewed, UniProtKB/Swiss-Prot Q6FXE3 (HEM1_CANGA)

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:	CAGL0B02607g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	530 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	? – 530		5-aminolevulinate synthase, mitochondrial		PRO_0000001238
Amino acid modifications
	Modified residue	319	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FXE3-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 0C5F159D8408A5D2	FASTA	530	58,385
	10 20 30 40 50 60 MFRPVLKVRP SFSYPYSIVS SRSVRLASTA TANANTAAAT STVAAHGTQE TPFDFEGHFE 70 80 90 100 110 120 SELAKKRLDK SYRYFNNINR LAKEFPLAHR QLEDDKVTVW CSNDYLALSK NPQVLDAMRK 130 140 150 160 170 180 TIDKYGAGAG GTRNIAGHNI PTMRLEAELA ALHKKEGALV FSSCYVANDA VISLLGQKVK 190 200 210 220 230 240 DLVIFSDELN HASMIVGIKH ANRPKHIFRH NDLAQLEEML QMYPKSTPKL IAFESVYSMA 250 260 270 280 290 300 GSVADINKIC DLAEKYGALT FLDEVHAVGL YGPHGAGVAE HCDFEAHRVA GIATPPQGDN 310 320 330 340 350 360 GRLRTVMDRV DMITGTLGKS FGTVGGYVAA SSKLIDWVRS YAPGFIFTTT LPPAVMAGAA 370 380 390 400 410 420 EAIRFQRSHL NLRQDQQRHT AYVKKGLHDL GIPVIPNPSH IVPVLIGNPD LAKQASDILM 430 440 450 460 470 480 EKHRIYVQAI NFPTVSRGTE RLRITPTPGH TNDLSDILIA AVDDVFNELQ LPRIRDWEMQ 490 500 510 520 530 GGLLGVGDKN FVPEPNLWTE EQLSFSNEDL NSNVFEPVID QLEVSSGVKL

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 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380948 Genomic DNA. Translation: CAG57984.1.
RefSeq	XP_445084.1.
3D structure databases
SMR	Q6FXE3. Positions 54-466, 141-497.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FXE3.
Genome annotation databases
GeneID	2886690.
GenomeReviews	Gene locus CAGL0B02607g in contig CR380948_GR.
KEGG	cgr:CAGL0B02607g.
Phylogenomic databases
eggNOG	fuNOG07159.
HOGENOM	HBG649839.
OMA	HLKESNE.
OrthoDB	EOG9CVHQ2.
PhylomeDB	Q6FXE3.
Enzyme and pathway databases
BRENDA	2.3.1.37. 189220.
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_CANGA

Accession

Primary (citable) accession number: Q6FXE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)