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P43089 (HEM1_PARDP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4094095-aminolevulinate synthase
PRO_0000163826

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: 7928952] [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.
+Additional computationally mapped references.

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...

Protein-protein interaction databases

STRINGP43089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4578534.
GenomeReviewsGene locus Pden_1822 in contig CP000489_GR.
KEGGpde:Pden_1822.
PATRIC22854745. VBIParDen97112_1755.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHBG649839.
PhylomeDBP43089.
ProtClustDBPRK09064.

Family and domain databases

InterProIPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KOK00643.
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_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: January 25, 2012
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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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