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Q92403 (HEM1_AGABI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismAgaricus bisporus (White button mushroom)
Taxonomic identifier5341 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetidae › Agaricales › Agaricaceae › Agaricus

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Biological processHeme biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function5-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 6215-aminolevulinate synthase, mitochondrialPRO_0000001235

Sites

Active site3621 By similarity
Binding site1221Substrate By similarity
Binding site2341Substrate By similarity
Binding site2861Pyridoxal phosphate By similarity
Binding site3141Pyridoxal phosphate By similarity
Binding site3591Pyridoxal phosphate By similarity
Binding site3911Pyridoxal phosphate By similarity
Binding site3921Pyridoxal phosphate By similarity
Binding site4771Substrate By similarity

Amino acid modifications

Modified residue3621N6-(pyridoxal phosphate)lysine Probable

Sequences

Sequence LengthMass (Da)Tools
Q92403 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: A335C3268FAE1AA3

FASTA62167,426
        10         20         30         40         50         60 
MSHHGPRLST RSQQIVAGYA SVAANFDVEK LHREQGVNIP TSGASINQCP HAAAARAAAR 

        70         80         90        100        110        120 
MADDLASAAR AKKSLDAKGS LAGRPVHHKA ATESTKAKHT GFDYEAFYKG ELAKKHQDKS 

       130        140        150        160        170        180 
YRYFNNINRL ARKFPVAHTA NPRDEVEVWC SNDYLGMGNN PVVLETMHRT LDKYGHGAGG 

       190        200        210        220        230        240 
TRNIAGNGAM HLGLERELRL HRKEAALVFS SCYVANDATL STLGTKLPGC VIFSDTMNHA 

       250        260        270        280        290        300 
SMIQGMRHST PKRVIFKHND LEDLETKLQQ YPKETPKIIA FESVYSMCGS IGPVKEICDL 

       310        320        330        340        350        360 
AEQYGAITFL DEVHAVGLYG PRGAGVAEHL DYDAHLAAGS SPDPIPGSVM DRIDIITGTL 

       370        380        390        400        410        420 
GKSYGAVGGY IAGSEEFVDM IRSYAPGFIF TTSLPPATVA GARASIVYQS EYLGDRQLKQ 

       430        440        450        460        470        480 
INVREVKRRL AELDIPVVPG SSHIVPVLVG DAALARAASD KLLSEHDIYV QAINYPTVAR 

       490        500        510        520        530        540 
GEERLRITVT PRHTMEQMEG LIRSLNQVFE ELNINRLSDW KLAGGRAGVG IPGAADDVQP 

       550        560        570        580        590        600 
IWTDEQIGLL NGTAPRSLRN AEKSVVDMRA VTIARSRFDV LLGPVYGELQ PTEDFDTPAV 

       610        620 
GATFKAPLVD REVAHDITVS A

« Hide

References

[1]Yague E., Mehak-Zunic M., Wood D.A., Thurston C.F.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: D649.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z50096 mRNA. Translation: CAA90424.1.

3D structure databases

ProteinModelPortalQ92403.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00251; UER00375.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR010961. 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]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01821. 5aminolev_synth. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_AGABI
AccessionPrimary (citable) accession number: Q92403
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: March 6, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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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