Reviewed, UniProtKB/Swiss-Prot O94069 (HEM1_CANAL)

Names and originHide

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
ORF Names:	Ca49C4.15, CaO19.2601

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributesHide

Sequence length	564 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)Hide

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.

OntologiesHide

Keywords
Biological process	Heme biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
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)Hide

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion
	Chain	? – 564		5-aminolevulinate synthase, mitochondrial		PRO_0000001237
Amino acid modifications
	Modified residue	353	1	N6-(pyridoxal phosphate)lysine Probable

SequencesHide

	Sequence		Length	Mass (Da)
	O94069-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: C984334068F40487	FASTA	564	61,395
	10 20 30 40 50 60 MESITKVSMS VCPFVRSTST QALRQLSQTS GALANQARQC PIAGNAIRAK EISIRSYSSA 70 80 90 100 110 120 TKPVRATAAT PSTPEATFNV SSSFELGSKE TAFDYNGYLG NELEKKRSDK SYRYFNNINR 130 140 150 160 170 180 LANEFPKAHR TQEEDKVTVW CSNDYLGMGK NENTLKEMKR VLDKYGSGAG GTRNIAGHNS 190 200 210 220 230 240 HAIKLESELA ALHKHDAALV FSSCFVANDA VLSLLGQKIK DLVIFSDELN HASMIQGIRN 250 260 270 280 290 300 SRARKHIFKH NNLADLESKL AQYPKSTPKL IAFESVYSMC GSIAPIEAIC DLAEKYGALT 310 320 330 340 350 360 FLDEVHAVGM YGPHGAGVAE HLNFEAHLKS GIERPEITTV MSRVDMVTGT LGKAYGVVGG 370 380 390 400 410 420 YITGKTNLID WFRSYAPGFI FTTSLPPAIM AGCSASIRYQ RATLKDRIAQ QKNTRLVKNN 430 440 450 460 470 480 LNELGIPVIP NPSHIVPVLV GNAADAKRAS DLLLNKHDIY VQAINFPTVP IGEERLRITP 490 500 510 520 530 540 TPGHGPELSK QLVEAVDSVF TELNLNRIND WKKLGGLVGV GVEGAAKVEH IWTEEQLALT 550 560 DADLNPNVVN PAISPLDVSS GIST

ReferencesHide

[1]	"Candida albicans strain 1161 genome pilot sequencing project." Murphy L., Harris D., Barrell B.G., Rajandream M.A. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1161.
[2]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.

Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	AL033503 Genomic DNA. Translation: CAA22025.1. AACQ01000044 Genomic DNA. Translation: EAK99337.1.
PIR	T18251.
RefSeq	XP_718266.1.
3D structure databases
SMR	O94069. Positions 94-500, 252-528.
ModBase	Search...
Genome annotation databases
GeneID	3640149.
KEGG	cal:CaO19.2601.
Organism-specific databases
CGD	CAL0003351. HEM1.
Phylogenomic databases
OMA	RAEKYIY.
OrthoDB	EOG9CVHQ2.
PhylomeDB	O94069.
Enzyme and pathway databases
BRENDA	2.3.1.37. 1124.
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]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01821. 5aminolev_synth. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry informationHide

Entry name

HEM1_CANAL

Accession

Primary (citable) accession number: O94069
Secondary accession number(s): Q5A965

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	July 13, 2010
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)