Reviewed, UniProtKB/Swiss-Prot P38092 (HEM1_EMENI)

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:	hemA
ORF Names:	AN2284

Organism

Emericella nidulans (Aspergillus nidulans) [Complete proteome]

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	648 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.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
Subcellular location	Mitochondrion matrix.
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
	Chain	? – 648		5-aminolevulinate synthase, mitochondrial		PRO_0000001240
Amino acid modifications
	Modified residue	412	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	300	1	A → R in CAA45508. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38092-1 [UniParc]. Last modified May 26, 2009. Version 2. Checksum: 1D450D773925F13F	FASTA	648	68,960
	10 20 30 40 50 60 MEALLQQSRA MCPFLKRSSP NTLRSLATAT RPSTSPGGGT MTNLQRIARR CPVMSKALAV 70 80 90 100 110 120 QSARMTGTKR FTSSAAGVPG AGAGTPKPTR GSPGKRALHS TGGNGANMST EFHKGAQQIH 130 140 150 160 170 180 PGLSNATRSH VGASATVSGP TPRAPVAAPF DYDAFYNAEL QKKHQDKSYR YFNNINRLAQ 190 200 210 220 230 240 EFPRAHTASK DEKVTVWCSN DYLGMGRNPE VLATMHKTLD TYGAGAGGTR NISGHNQHAV 250 260 270 280 290 300 SLENTLAKLH GKEAALVFSS CFVANDATLA TLGSKMPDCV ILSDSLNHAS MIQGIRHSGA 310 320 330 340 350 360 KKMVFKHNDL VDLETKLASL PLHVPKIIAF ESVYSMCGSI APIEAICDLA DKYGAITFLD 370 380 390 400 410 420 EVHAVGMYGP HGAGVAEHLD YEIYASQDTA NPLSTKGTVM DRINIITGTL GKAYGCVGGY 430 440 450 460 470 480 IAGSAALVDT IRSLAPGFIF TTSLPPATMA GADTAIRYQA RHQQDRILQQ LHTRAVKQSF 490 500 510 520 530 540 KDLDIPVIPN PSHIVPLLVG DAELAKQASD KLLEEHGIYV QAINYPTVPR GEERLRITPT 550 560 570 580 590 600 PGHTQELRDH LVEAVNTVWN DLGIKRASDW KAMGGFVGVG VEAAELENQP IWTDAQLNMR 610 620 630 640 PDETLEAAVE REFQAAVPGM KAGGAKAKPV GSIAANPIGA SIPVAAAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and nucleotide sequence of the 5-aminolevulinate synthase gene from Aspergillus nidulans." Bradshaw R.E., Dixon S.W.C., Raitt D.C., Pillar T.M. Curr. Genet. 23:501-507(1993) [PubMed: 8319309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: R153.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X64170 Genomic DNA. Translation: CAA45508.1. AACD01000038 Genomic DNA. Translation: EAA64395.1.
PIR	S31846.
RefSeq	XP_659888.1.
3D structure databases
HSSP	HSSP built from PDB template 1FC4 based on UniProtKB P07912.
ModBase	Search...
Genome annotation databases
GeneID	2874789.
KEGG	ani:AN2284.2.
Enzyme and pathway databases
BRENDA	2.3.1.37. 3859.
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_EMENI

Accession

Primary (citable) accession number: P38092
Secondary accession number(s): Q5BAZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	May 26, 2009
Last modified:	September 22, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)