5-aminolevulinate synthase, mitochondrial precursor - Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast)

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Q6FXE3 (HEM1_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	HEM1
Ordered Locus Names:	CAGL0B02607g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces ›

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO₂.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Biological process	Heme biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	5-aminolevulinate synthase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion Potential

Chain

? – 530

5-aminolevulinate synthase, mitochondrial

PRO_0000001238

Sites

Active site

1

By similarity

Binding site

1

Substrate By similarity

Binding site

1

Substrate By similarity

Binding site

1

Substrate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Substrate By similarity

Amino acid modifications

Modified residue

1

N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6FXE3 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 0C5F159D8408A5D2
Show »

530

58,385

        10         20         30         40         50         60 
MFRPVLKVRP SFSYPYSIVS SRSVRLASTA TANANTAAAT STVAAHGTQE TPFDFEGHFE 

        70         80         90        100        110        120 
SELAKKRLDK SYRYFNNINR LAKEFPLAHR QLEDDKVTVW CSNDYLALSK NPQVLDAMRK 

       130        140        150        160        170        180 
TIDKYGAGAG GTRNIAGHNI PTMRLEAELA ALHKKEGALV FSSCYVANDA VISLLGQKVK 

       190        200        210        220        230        240 
DLVIFSDELN HASMIVGIKH ANRPKHIFRH NDLAQLEEML QMYPKSTPKL IAFESVYSMA 

       250        260        270        280        290        300 
GSVADINKIC DLAEKYGALT FLDEVHAVGL YGPHGAGVAE HCDFEAHRVA GIATPPQGDN 

       310        320        330        340        350        360 
GRLRTVMDRV DMITGTLGKS FGTVGGYVAA SSKLIDWVRS YAPGFIFTTT LPPAVMAGAA 

       370        380        390        400        410        420 
EAIRFQRSHL NLRQDQQRHT AYVKKGLHDL GIPVIPNPSH IVPVLIGNPD LAKQASDILM 

       430        440        450        460        470        480 
EKHRIYVQAI NFPTVSRGTE RLRITPTPGH TNDLSDILIA AVDDVFNELQ LPRIRDWEMQ 

       490        500        510        520        530 
GGLLGVGDKN FVPEPNLWTE EQLSFSNEDL NSNVFEPVID QLEVSSGVKL

References

[1]

"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.

expand/collapse author list

Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR380948 Genomic DNA. Translation: CAG57984.1.
RefSeq	XP_445084.1. XM_445084.1.
3D structure databases
ProteinModelPortal	Q6FXE3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2886690.
KEGG	cgr:CAGL0B02607g.
Phylogenomic databases
HOGENOM	HOG000221020.
KO	K00643.
OMA	HANKQIV.
OrthoDB	EOG412QDQ.
Enzyme and pathway databases
UniPathway	UPA00251; UER00375.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR010961. 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]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01821. 5aminolev_synth. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_CANGA

Accession

Primary (citable) accession number: Q6FXE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents