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Protein

5-aminolevulinate synthase, mitochondrial

Gene

HEM1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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), 5-aminolevulinate synthase (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 sitei113SubstrateBy similarity1
Binding sitei226SubstrateBy similarity1
Binding sitei245SubstrateBy similarity1
Binding sitei278Pyridoxal phosphateBy similarity1
Binding sitei306Pyridoxal phosphateBy similarity1
Binding sitei350Pyridoxal phosphateBy similarity1
Active sitei353By similarity1
Binding sitei382Pyridoxal phosphate; shared with dimeric partnerBy similarity1
Binding sitei383Pyridoxal phosphate; shared with dimeric partnerBy similarity1
Binding sitei468SubstrateBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • heme biosynthetic process Source: CGD
  • 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

UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase, mitochondrial (EC:2.3.1.37)
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene namesi
Name:HEM1
ORF Names:Ca49C4.15, CaO19.2601
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0000189686. HEM1.
EuPathDBiFungiDB:CR_02000C_A.

Subcellular locationi

  • Mitochondrion matrix By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 57MitochondrionSequence analysisAdd BLAST57
ChainiPRO_000000123758 – 5645-aminolevulinate synthase, mitochondrialAdd BLAST507

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei353N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PRIDEiO94069.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO94069.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiO94069.
KOiK00643.
OrthoDBiEOG092C1OK6.

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.

O94069-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESITKVSMS VCPFVRSTST QALRQLSQTS GALANQARQC PIAGNAIRAK
60 70 80 90 100
EISIRSYSSA TKPVRATAAT PSTPEATFNV SSSFELGSKE TAFDYNGYLG
110 120 130 140 150
NELEKKRSDK SYRYFNNINR LANEFPKAHR TQEEDKVTVW CSNDYLGMGK
160 170 180 190 200
NENTLKEMKR VLDKYGSGAG GTRNIAGHNS HAIKLESELA ALHKHDAALV
210 220 230 240 250
FSSCFVANDA VLSLLGQKIK DLVIFSDELN HASMIQGIRN SRARKHIFKH
260 270 280 290 300
NNLADLESKL AQYPKSTPKL IAFESVYSMC GSIAPIEAIC DLAEKYGALT
310 320 330 340 350
FLDEVHAVGM YGPHGAGVAE HLNFEAHLKS GIERPEITTV MSRVDMVTGT
360 370 380 390 400
LGKAYGVVGG YITGKTNLID WFRSYAPGFI FTTSLPPAIM AGCSASIRYQ
410 420 430 440 450
RATLKDRIAQ QKNTRLVKNN LNELGIPVIP NPSHIVPVLV GNAADAKRAS
460 470 480 490 500
DLLLNKHDIY VQAINFPTVP IGEERLRITP TPGHGPELSK QLVEAVDSVF
510 520 530 540 550
TELNLNRIND WKKLGGLVGV GVEGAAKVEH IWTEEQLALT DADLNPNVVN
560
PAISPLDVSS GIST
Length:564
Mass (Da):61,395
Last modified:May 1, 1999 - v1
Checksum:iC984334068F40487
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL033503 Genomic DNA. Translation: CAA22025.1.
AACQ01000044 Genomic DNA. Translation: EAK99337.1.
PIRiT18251.
RefSeqiXP_718266.1. XM_713173.1.

Genome annotation databases

EnsemblFungiiEAK99337; EAK99337; CaO19.2601.
GeneIDi3640149.
KEGGical:CaO19.2601.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL033503 Genomic DNA. Translation: CAA22025.1.
AACQ01000044 Genomic DNA. Translation: EAK99337.1.
PIRiT18251.
RefSeqiXP_718266.1. XM_713173.1.

3D structure databases

ProteinModelPortaliO94069.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO94069.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAK99337; EAK99337; CaO19.2601.
GeneIDi3640149.
KEGGical:CaO19.2601.

Organism-specific databases

CGDiCAL0000189686. HEM1.
EuPathDBiFungiDB:CR_02000C_A.

Phylogenomic databases

InParanoidiO94069.
KOiK00643.
OrthoDBiEOG092C1OK6.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.

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...

Entry informationi

Entry nameiHEM1_CANAL
AccessioniPrimary (citable) accession number: O94069
Secondary accession number(s): Q5A965
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 108 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. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.