Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

5-aminolevulinate synthase, mitochondrial

Gene

hem1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei152SubstrateBy similarity1
Binding sitei265SubstrateBy similarity1
Binding sitei284SubstrateBy similarity1
Binding sitei317Pyridoxal phosphateBy similarity1
Binding sitei345Pyridoxal phosphateBy similarity1
Binding sitei374Pyridoxal phosphateBy similarity1
Active sitei377By similarity1
Binding sitei406Pyridoxal phosphate; shared with dimeric partnerBy similarity1
Binding sitei407Pyridoxal phosphate; shared with dimeric partnerBy similarity1
Binding sitei492SubstrateBy similarity1

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

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processHeme biosynthesis
LigandPyridoxal 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 25MitochondrionSequence analysisAdd BLAST25
ChainiPRO_000000124326 – 5585-aminolevulinate synthase, mitochondrialAdd BLAST533

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei377N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

MaxQBiO14092
PaxDbiO14092
PRIDEiO14092

PTM databases

iPTMnetiO14092

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi278510, 3 interactors
STRINGi4896.SPAC2F3.09.1

Structurei

3D structure databases

ProteinModelPortaliO14092
SMRiO14092
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000221020
InParanoidiO14092
KOiK00643
OMAiKQDHTYR
OrthoDBiEOG092C1OK6
PhylomeDBiO14092

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
InterProiView protein in InterPro
IPR010961 4pyrrol_synth_NH2levulA_synth
IPR001917 Aminotrans_II_pyridoxalP_BS
IPR004839 Aminotransferase_I/II
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR01821 5aminolev_synth, 1 hit
PROSITEiView protein in PROSITE
PS00599 AA_TRANSFER_CLASS_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiHEM1_SCHPO
AccessioniPrimary (citable) accession number: O14092
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 1, 1998
Last modified: February 28, 2018
This is version 117 of the entry and version 1 of the sequence. See 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health