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Protein

5-aminolevulinate synthase, mitochondrial

Gene

HEM1

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731SubstrateBy similarity
Binding sitei186 – 1861SubstrateBy similarity
Binding sitei205 – 2051SubstrateBy similarity
Binding sitei238 – 2381Pyridoxal phosphateBy similarity
Binding sitei266 – 2661Pyridoxal phosphateBy similarity
Binding sitei316 – 3161Pyridoxal phosphateBy similarity
Active sitei319 – 3191By similarity
Binding sitei348 – 3481Pyridoxal phosphateBy similarity
Binding sitei349 – 3491Pyridoxal phosphateBy similarity
Binding sitei434 – 4341SubstrateBy similarity

GO - Molecular functioni

  1. 5-aminolevulinate synthase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. 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
Ordered Locus Names:CAGL0B02607g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
ProteomesiUP000002428 Componenti: Chromosome B

Organism-specific databases

EuPathDBiFungiDB:CAGL0B02607g.

Subcellular locationi

  1. Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 5305-aminolevulinate synthase, mitochondrialPRO_0000001238
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei319 – 3191N6-(pyridoxal phosphate)lysineBy similarity

Structurei

3D structure databases

ProteinModelPortaliQ6FXE3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000221020.
InParanoidiQ6FXE3.
KOiK00643.
OMAiRAEKYIY.
OrthoDBiEOG7HHX1P.

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.

Q6FXE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRPVLKVRP SFSYPYSIVS SRSVRLASTA TANANTAAAT STVAAHGTQE
60 70 80 90 100
TPFDFEGHFE SELAKKRLDK SYRYFNNINR LAKEFPLAHR QLEDDKVTVW
110 120 130 140 150
CSNDYLALSK NPQVLDAMRK TIDKYGAGAG GTRNIAGHNI PTMRLEAELA
160 170 180 190 200
ALHKKEGALV FSSCYVANDA VISLLGQKVK DLVIFSDELN HASMIVGIKH
210 220 230 240 250
ANRPKHIFRH NDLAQLEEML QMYPKSTPKL IAFESVYSMA GSVADINKIC
260 270 280 290 300
DLAEKYGALT FLDEVHAVGL YGPHGAGVAE HCDFEAHRVA GIATPPQGDN
310 320 330 340 350
GRLRTVMDRV DMITGTLGKS FGTVGGYVAA SSKLIDWVRS YAPGFIFTTT
360 370 380 390 400
LPPAVMAGAA EAIRFQRSHL NLRQDQQRHT AYVKKGLHDL GIPVIPNPSH
410 420 430 440 450
IVPVLIGNPD LAKQASDILM EKHRIYVQAI NFPTVSRGTE RLRITPTPGH
460 470 480 490 500
TNDLSDILIA AVDDVFNELQ LPRIRDWEMQ GGLLGVGDKN FVPEPNLWTE
510 520 530
EQLSFSNEDL NSNVFEPVID QLEVSSGVKL
Length:530
Mass (Da):58,385
Last modified:July 19, 2004 - v1
Checksum:i0C5F159D8408A5D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380948 Genomic DNA. Translation: CAG57984.1.
RefSeqiXP_445084.1. XM_445084.1.

Genome annotation databases

GeneIDi2886690.
KEGGicgr:CAGL0B02607g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380948 Genomic DNA. Translation: CAG57984.1.
RefSeqiXP_445084.1. XM_445084.1.

3D structure databases

ProteinModelPortaliQ6FXE3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2886690.
KEGGicgr:CAGL0B02607g.

Organism-specific databases

EuPathDBiFungiDB:CAGL0B02607g.

Phylogenomic databases

HOGENOMiHOG000221020.
InParanoidiQ6FXE3.
KOiK00643.
OMAiRAEKYIY.
OrthoDBiEOG7HHX1P.

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_CANGA
AccessioniPrimary (citable) accession number: Q6FXE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 19, 2004
Last modified: April 29, 2015
This is version 77 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.