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P43090 (HEM0_OPSTA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 78. 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, erythroid-specific, mitochondrial
Short name=ALAS-E
EC=2.3.1.37
Alternative name(s):
5-aminolevulinic acid synthase 2
Delta-ALA synthase 2
Delta-aminolevulinate synthase 2
Gene names
Name:alas2
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 length582 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 5825-aminolevulinate synthase, erythroid-specific, mitochondrialPRO_0000001228

Sites

Active site3861 By similarity
Binding site1581Substrate By similarity
Binding site2751Substrate By similarity
Binding site3271Pyridoxal phosphate By similarity
Binding site3551Pyridoxal phosphate By similarity
Binding site3831Pyridoxal phosphate By similarity
Binding site4151Pyridoxal phosphate By similarity
Binding site4161Pyridoxal phosphate By similarity
Binding site5031Substrate By similarity

Amino acid modifications

Modified residue3861N6-(pyridoxal phosphate)lysine Probable

Sequences

Sequence LengthMass (Da)Tools
P43090 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: FB066EEF72E146C9

FASTA58264,531
        10         20         30         40         50         60 
MAAFLHHCPF LKSMPKPALR RRVPALLSLA DRCPVIVHQV CISRLHILET KLDVSPTQPK 

        70         80         90        100        110        120 
RQRLSLLDQK RLFAQTATQV AVSVSKGCPF VSSQIGMVRA SPEVQEDVQA DLKSPVLPTP 

       130        140        150        160        170        180 
PQTGITQLLK DNMVGPSFDY DNFFNEKIAE KKRDHTYRVF KTVNRNAVVF PFAEDYSVSD 

       190        200        210        220        230        240 
RQGSQVSVWC SNDYLGMSRH PRVLEAIREV LERHGAGAGG TRNISGTSKY HVTLEKELAH 

       250        260        270        280        290        300 
LHQKDAALVF SSCFVANDST LFTLAKMLPG CHIYSDAGNH ASMIQGIRNS GAKRFIFRHN 

       310        320        330        340        350        360 
DSRHLEELLQ QSDPKTPKIV AFETVHSMDG AICPLEELCD VAHRHGALTF VDEVHAVGLY 

       370        380        390        400        410        420 
GAHGAGVGER DNVMHKIDIV SGTLGKAFGC VGGYVASSAA LVDTVRSFAA GFIFTTSLPP 

       430        440        450        460        470        480 
MILAGALESV RVLKSPEGQL LRRAHQRNVK YMRQLLMDKG LPVVNCPSHI IPIRVGNAEL 

       490        500        510        520        530        540 
NTKVCDSLLE KHNIYVQAIN YPTVPRGQEL LRLAPSPHHH PAMMEYFVDK LVEVWQEAGL 

       550        560        570        580 
LLNGPATVSC TFCDRPLHFD LMSEWEKSYF GNMEPQYITM SA

« Hide

References

[1]"5-aminolevulinate synthase in the marine fish, Opsanus tau."
Hellmich H.L., Cornell N.W.
Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L02632 mRNA. Translation: AAA60729.1.

3D structure databases

ProteinModelPortalP43090.
SMRP43090. Positions 139-535.
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 nameHEM0_OPSTA
AccessionPrimary (citable) accession number: P43090
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 6, 2013
This is version 78 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

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