Skip Header

Contribute Send feedback
Read comments (?) or add your own

P43091 (HEM1_OPSTA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-aminolevulinate synthase, nonspecific, mitochondrial
Short name=ALAS-H
EC=2.3.1.37
Alternative name(s):
5-aminolevulinic acid synthase 1
Delta-ALA synthase 1
Delta-aminolevulinate synthase 1
Gene names
Name:alas1
OrganismOpsanus tau (Oyster toadfish) (Gadus tau)
Taxonomic identifier8068 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Paracanthopterygii › Batrachoididae › Opsanus

Protein attributes

Sequence length627 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.

Miscellaneous

There are two delta-ALA synthases in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues.

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 – 5858Mitochondrion Potential
Chain59 – 6275695-aminolevulinate synthase, nonspecific, mitochondrial
PRO_0000001234

Sites

Active site4321 By similarity
Binding site2041Substrate By similarity
Binding site3211Substrate By similarity
Binding site3401Substrate By similarity
Binding site3731Pyridoxal phosphate By similarity
Binding site4011Pyridoxal phosphate By similarity
Binding site4291Pyridoxal phosphate By similarity
Binding site4611Pyridoxal phosphate By similarity
Binding site4621Pyridoxal phosphate By similarity
Binding site5491Substrate By similarity

Amino acid modifications

Modified residue4321N6-(pyridoxal phosphate)lysine Probable

Sequences

Sequence LengthMass (Da)Tools
P43091 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: B94FB3406D9FCCAF

FASTA62769,691
        10         20         30         40         50         60 
MDVIVRRCPF LARVPQAFFQ QSKKSLAVYA QRCPFMMELA SKPMAPSLAR ALCSSSSSQQ 

        70         80         90        100        110        120 
KIEDTMSTGE VLKPKAEAKL PVGLATPPSN EAVAPKCPFL AAEMGQNNSN VVRQVGVEFQ 

       130        140        150        160        170        180 
EDVEEIRTVQ KEVSPAQLEQ PSLIGKTMGE EGHQKNLMKS LLKQRPKRVS HLLQDNLPGS 

       190        200        210        220        230        240 
FTRFYYDNFF EKKIEEKKSD HTYRVFKTVN RLANEFPMAD DFTGSLEDKR EVSVWCSNDY 

       250        260        270        280        290        300 
LGMSRHPRVA QAIMETLRKH GSGAGGTRNI SGTSKFHVEL EQELADLHRK DAALLFTSCF 

       310        320        330        340        350        360 
VANDSTLFTL AKMLPGCEIY SDAGNHASMI QGIRNSGAKK FIFRHNDVAH LRELLEKGDP 

       370        380        390        400        410        420 
TKPKIVAFET VHSMDGAVCP LEEMCDLAHE FGAITFVDEV HAVGLYGPRG GGIGDRDGIM 

       430        440        450        460        470        480 
HKMDIISGTL GKAFGCVGGY IASTATLVDT VRSYAAGFIF TTSLPPMLLA GAKQSIQILK 

       490        500        510        520        530        540 
GEEGCTLRRK HQRNVKLLRQ MLMDSGLPVV HCPSHIIPIR VSDAEKNTKV CDLMMSHHNI 

       550        560        570        580        590        600 
YVQAINYPTV ARGDELLRIA PTPHHTPEMM KYFVDRLVQT WKEVGLELKP HSSAECTFCQ 

       610        620 
QPLHFEVMNE REKSYFSGLS HLVSVCA

« Hide

References

[1]"Housekeeping form of 5-aminolevulinate synthase in the marine fish, Opsanus tau."
Cornell N.W.
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L35915 mRNA. Translation: AAA49435.1.

3D structure databases

ProteinModelPortalP43091.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005954.

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.
IPR015118. 5aminolev_synth_preseq.
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.
PF09029. Preseq_ALAS. 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_OPSTA
AccessionPrimary (citable) accession number: P43091
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 6, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents