Reviewed, UniProtKB/Swiss-Prot O14092 (HEM1_SCHPO)

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
ORF Names:	SPAC2F3.09

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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	? – 558		5-aminolevulinate synthase, mitochondrial		PRO_0000001243
Amino acid modifications
	Modified residue	377	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O14092-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: C599FE2B91F3BD3D	FASTA	558	60,960
	10 20 30 40 50 60 MERVVKLAAK HCPFVSKADP SALRRMAGAG LIRAGARCPV VRHALPVAAA TGADVSRGFK 70 80 90 100 110 120 SDSKQMAMEP SLDEIHLKAG VVNTGSRTCR HADAVKAAAE AATTTPVTKK HQMPKHYASD 130 140 150 160 170 180 LNGVGPATTP RFDYDTFYRE ELDKKHRDKS YRYFNNINRL AKEYPLAHLA DPNTRVEVWC 190 200 210 220 230 240 SNDYLNMGGH KKIREAMHQC IETYGGGAGG TRNIAGHNQH AVRLEKSLAD LHQKPAALVF 250 260 270 280 290 300 GSCYVANDAT LSTLGRKLPN CIFLSDEMNH ASMINGIRNS RCEKIIFKHN DLVDLEAKLA 310 320 330 340 350 360 SLPLNRPKII AFESVYSMSG NVAPISEICD LAKKYGAITF LDEVHAVGMY GPRGAGVAEE 370 380 390 400 410 420 TPGLLSRVDI ITGTLAKSYG CVGGYIAASS TLVDMIRSLA PGFIFTTSLP PHVMVGALTA 430 440 450 460 470 480 VEHLKVSNVE REQQRSAVRR VKQSLSEIGI PVLSNDTHIV PAMVGDAHLA KLASDSLLHD 490 500 510 520 530 540 HNIYVQSINF PTVSVGTERL RITPTPAHNT EHYVQSLTNA MNDVWSKFNI NRIDGWEKRG 550 IDVGRLCKFP VLPFTTTH

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB16265.1.
PIR	T38542.
RefSeq	NP_594388.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O14092.
Genome annotation databases
GeneID	2542028.
GenomeReviews	Gene locus hem1 in contig CU329670_GR.
KEGG	spo:SPAC2F3.09.
NMPDR	fig|4896.1.peg.4358.
Organism-specific databases
GeneDB_Spombe	SPAC2F3.09.
Phylogenomic databases
OMA	AVWTRPD.
Enzyme and pathway databases
BRENDA	2.3.1.37. 653.
Gene expression databases
ArrayExpress	O14092.
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_SCHPO

Accession

Primary (citable) accession number: O14092

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)