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P43089 (HEM1_PARDP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 83. 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

Names and origin

Protein namesRecommended name:
5-aminolevulinate synthase

EC=2.3.1.37
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene names
Name:hemA
Ordered Locus Names:Pden_1822
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Pathway

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

Sequence similarities

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

Sequence caution

The sequence ABL69919.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHeme biosynthesis
   LigandPyridoxal phosphate
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_function5-aminolevulinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4094095-aminolevulinate synthase
PRO_0000163826

Sites

Active site2481 By similarity
Binding site211Substrate By similarity
Binding site1371Substrate By similarity
Binding site1561Substrate By similarity
Binding site1891Pyridoxal phosphate By similarity
Binding site2171Pyridoxal phosphate By similarity
Binding site2451Pyridoxal phosphate By similarity
Binding site2771Pyridoxal phosphate By similarity
Binding site2781Pyridoxal phosphate By similarity
Binding site3651Substrate By similarity

Amino acid modifications

Modified residue2481N6-(pyridoxal phosphate)lysine Probable

Experimental info

Sequence conflict351Q → T in AAA62279. Ref.1
Sequence conflict1011S → A in AAA62279. Ref.1
Sequence conflict1151A → V in AAA62279. Ref.1
Sequence conflict152 – 1554FDGA → STAP in AAA62279. Ref.1
Sequence conflict1651A → G in AAA62279. Ref.1
Sequence conflict1951G → A in AAA62279. Ref.1
Sequence conflict1991A → E in AAA62279. Ref.1
Sequence conflict2471G → A in AAA62279. Ref.1
Sequence conflict258 – 2603AAS → GFG in AAA62279. Ref.1
Sequence conflict2881A → V in AAA62279. Ref.1
Sequence conflict302 – 3032LL → FV in AAA62279. Ref.1
Sequence conflict311 – 3133ARI → GRL in AAA62279. Ref.1
Sequence conflict3211L → A in AAA62279. Ref.1
Sequence conflict3251I → V in AAA62279. Ref.1
Sequence conflict3551G → S in AAA62279. Ref.1
Sequence conflict3771P → A in AAA62279. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P43089 [UniParc].

Last modified March 6, 2007. Version 2.
Checksum: 1A2EEE178D58B32E

FASTA40944,560
        10         20         30         40         50         60 
MDYSAALDQA IGKLHEEGRY RTFIDIERRK GAYPQAVWTR PDGTETRITV WCGNDYLGMG 

        70         80         90        100        110        120 
QHPVVLAAMH EALDATGAGS GGTRNISGTT VYHKRLEAEL SDLHGKEAAL VFSSAYIAND 

       130        140        150        160        170        180 
ATLSTLRKLF PGLIIYSDEL NHASMIEGIK RFDGAKRIFR HNDVAHLREL LAADDPEAPK 

       190        200        210        220        230        240 
LIAFESIYSM DGDFGPIKAI CDLADEFNAL TYLDEVHAVG MYGPRGGGVA ERDGLSHRID 

       250        260        270        280        290        300 
IFNGTLGKAF GVFGGYIAAS ARMVDAIRSY APGFIFTTSL PPAVAAGAAA SIAFLKTAEG 

       310        320        330        340        350        360 
QLLRDQQQLN ARILKMRLRG LGMPIMDHGS HIVPVHVGNP VHCKALSDML LADFGIYVQP 

       370        380        390        400 
INFPTVPRGT ERLRFTPSPV HDPKQIDHLV KAMDSLWSQC KLNRSTSAA 

« Hide

References

« Hide 'large scale' references
[1]"Differential reduction in soluble and membrane-bound c-type cytochrome contents in a Paracoccus denitrificans mutant partially deficient in 5-aminolevulinate synthase activity."
Page M.D., Ferguson S.J.
J. Bacteriol. 176:5919-5928(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12508 Genomic DNA. Translation: AAA62279.1.
CP000489 Genomic DNA. Translation: ABL69919.1. Different initiation.
RefSeqYP_915615.1. NC_008686.1.

3D structure databases

ProteinModelPortalP43089.
SMRP43089. Positions 1-397.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318586.Pden_1822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL69919; ABL69919; Pden_1822.
GeneID4578534.
KEGGpde:Pden_1822.
PATRIC22854745. VBIParDen97112_1755.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000221020.
KOK00643.
OrthoDBEOG6Q8HZD.
ProtClustDBPRK09064.

Enzyme and pathway databases

BioCycPDEN318586:GCVQ-1848-MONOMER.
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. SSF53383. 1 hit.
TIGRFAMsTIGR01821. 5aminolev_synth. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_PARDP
AccessionPrimary (citable) accession number: P43089
Secondary accession number(s): A1B325
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: March 6, 2007
Last modified: November 13, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways