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Protein

5-aminolevulinate synthase, mitochondrial

Gene

HEM1

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
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 sitei119 – 1191SubstrateBy similarity
Binding sitei232 – 2321SubstrateBy similarity
Binding sitei251 – 2511SubstrateBy similarity
Binding sitei284 – 2841Pyridoxal phosphateBy similarity
Binding sitei312 – 3121Pyridoxal phosphateBy similarity
Binding sitei356 – 3561Pyridoxal phosphateBy similarity
Active sitei359 – 3591By similarity
Binding sitei388 – 3881Pyridoxal phosphateBy similarity
Binding sitei389 – 3891Pyridoxal phosphateBy similarity
Binding sitei474 – 4741SubstrateBy 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:KLLA0C15059g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598: Chromosome C

Subcellular locationi

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? – 5705-aminolevulinate synthase, mitochondrialPRO_0000001241
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei359 – 3591N6-(pyridoxal phosphate)lysineCurated

Interactioni

Protein-protein interaction databases

STRINGi28985.P78698.

Structurei

3D structure databases

ProteinModelPortaliP78698.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221020.
InParanoidiP78698.
KOiK00643.
OMAiCERQIWR.
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.

P78698-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESVIRSSAK ICPFMHSATG SMQSVKALKN ANLPAIAQQC PFMGKAMEQR
60 70 80 90 100
RGYASSASGA SAAAAATATA STSASNSNSS VEASASADVV DHATKEASFD
110 120 130 140 150
YQGLFDSDLA KKRMDKSYRF FNNINRLAKE FPMAHRKLED DKVTVWCSND
160 170 180 190 200
YLALSKNQEV IEVMKKTLDK YGAGAGGTRN IAGHNKHALQ LEAELATLHK
210 220 230 240 250
KEGALVFSSC FVANDAVISL LGQKIKDLVI FSDELNHASM IVGIKHASTK
260 270 280 290 300
KHIFKHNNLD QLEELLAMYP KSTPKLIAFE SVYSMSGSVA DIDKICDLAE
310 320 330 340 350
KYGALTFLDE VHAVGLYGPH GAGVAEHCNF DAHRKAGIAS PEFRTVMDRV
360 370 380 390 400
DMITGTLGKS FGTVGGYVAG SLQLIDWVRS YAPGFIFTTT LPPAVMAGAA
410 420 430 440 450
EAIRYQRSHL DLRQDQQRHT TYVKDGLADL GIPVMPNPSH IVPVLVGNPH
460 470 480 490 500
LAKQASDILM DKHRIYVQAI NFPTVARGTE RLRITPTPGH TNDLSDILMD
510 520 530 540 550
ALEDVWSTLQ LPRVRDWEAQ GGLLGVGDPN HVPQPNLWTK DQLTLTNNDL
560 570
HPNVKQPIIE QLEVSSGIRY
Length:570
Mass (Da):62,139
Last modified:September 27, 2004 - v2
Checksum:iCD9151C4A529AA89
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti332 – 3321A → R in CAA63497. (PubMed:9271110)Curated
Sequence conflicti487 – 4871T → S in CAA63497. (PubMed:9271110)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92944 Genomic DNA. Translation: CAA63497.1.
CR382123 Genomic DNA. Translation: CAH01726.1.
RefSeqiXP_452875.1. XM_452875.1.

Genome annotation databases

GeneIDi2892616.
KEGGikla:KLLA0C15059g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92944 Genomic DNA. Translation: CAA63497.1.
CR382123 Genomic DNA. Translation: CAH01726.1.
RefSeqiXP_452875.1. XM_452875.1.

3D structure databases

ProteinModelPortaliP78698.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi28985.P78698.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2892616.
KEGGikla:KLLA0C15059g.

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221020.
InParanoidiP78698.
KOiK00643.
OMAiCERQIWR.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the KlHEM1 gene in Kluyveromyces lactis."
    Gonzales-Dominguez M., Mendez-Carro C., Cerdan M.E.
    Yeast 13:961-971(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
  2. "Genome evolution in yeasts."
    Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
    Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Entry informationi

Entry nameiHEM1_KLULA
AccessioniPrimary (citable) accession number: P78698
Secondary accession number(s): Q6CT64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 27, 2004
Last modified: January 7, 2015
This is version 103 of the entry and version 2 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.