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Protein

5-aminolevulinate synthase, mitochondrial

Gene

hem1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.By similarity

Catalytic activityi

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.By similarity

Cofactori

pyridoxal 5'-phosphateBy similarity

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from glycine.By similarity
Proteins known to be involved in this subpathway in this organism are:
  1. 5-aminolevulinate synthase, mitochondrial (hem1)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from glycine, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei152 – 1521SubstrateBy similarity
Binding sitei265 – 2651SubstrateBy similarity
Binding sitei284 – 2841SubstrateBy similarity
Binding sitei317 – 3171Pyridoxal phosphateBy similarity
Binding sitei345 – 3451Pyridoxal phosphateBy similarity
Binding sitei374 – 3741Pyridoxal phosphateBy similarity
Active sitei377 – 3771By similarity
Binding sitei406 – 4061Pyridoxal phosphate; shared with dimeric partnerBy similarity
Binding sitei407 – 4071Pyridoxal phosphate; shared with dimeric partnerBy similarity
Binding sitei492 – 4921SubstrateBy similarity

GO - Molecular functioni

  • 5-aminolevulinate synthase activity Source: PomBase
  • pyridoxal phosphate binding Source: InterPro
  • transaminase activity Source: PomBase

GO - Biological processi

  • heme biosynthetic process Source: PomBase
  • protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-SPO-189451. Heme biosynthesis.
UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase, mitochondrial1 Publication (EC:2.3.1.37)
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene namesi
Name:hem11 Publication
ORF Names:SPAC2F3.09
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC2F3.09.
PomBaseiSPAC2F3.09. hem1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: PomBase
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Lethal, unless exogenous ALA is provided, allowing heme biosynthesis from step 2 to proceed. An additional way to maintain cells alive is to add exogenous hemin (heme chloride), thereby fostering cells to use their heme uptake system.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionSequence analysisAdd
BLAST
Chaini26 – 5585335-aminolevulinate synthase, mitochondrialPRO_0000001243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei377 – 3771N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

MaxQBiO14092.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi278510. 2 interactions.
MINTiMINT-4670412.

Structurei

3D structure databases

ProteinModelPortaliO14092.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000221020.
InParanoidiO14092.
KOiK00643.
OMAiMPGCVIL.
OrthoDBiEOG7HHX1P.
PhylomeDBiO14092.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O14092-1 [UniParc]FASTAAdd to basket

« Hide

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

VLPFTTTH
Length:558
Mass (Da):60,960
Last modified:January 1, 1998 - v1
Checksum:iC599FE2B91F3BD3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16265.1.
PIRiT38542.
RefSeqiNP_594388.1. NM_001019809.2.

Genome annotation databases

EnsemblFungiiSPAC2F3.09.1; SPAC2F3.09.1:pep; SPAC2F3.09.
GeneIDi2542028.
KEGGispo:SPAC2F3.09.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16265.1.
PIRiT38542.
RefSeqiNP_594388.1. NM_001019809.2.

3D structure databases

ProteinModelPortaliO14092.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278510. 2 interactions.
MINTiMINT-4670412.

Proteomic databases

MaxQBiO14092.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC2F3.09.1; SPAC2F3.09.1:pep; SPAC2F3.09.
GeneIDi2542028.
KEGGispo:SPAC2F3.09.

Organism-specific databases

EuPathDBiFungiDB:SPAC2F3.09.
PomBaseiSPAC2F3.09. hem1.

Phylogenomic databases

HOGENOMiHOG000221020.
InParanoidiO14092.
KOiK00643.
OMAiMPGCVIL.
OrthoDBiEOG7HHX1P.
PhylomeDBiO14092.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.
ReactomeiR-SPO-189451. Heme biosynthesis.

Miscellaneous databases

NextBioi20803106.
PROiO14092.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  3. "Shu1 is a cell-surface protein involved in iron acquisition from heme in Schizosaccharomyces pombe."
    Mourer T., Jacques J.F., Brault A., Bisaillon M., Labbe S.
    J. Biol. Chem. 290:10176-10190(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiHEM1_SCHPO
AccessioniPrimary (citable) accession number: O14092
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 1, 1998
Last modified: November 11, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.