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P18079 (HEM1_RHOCB) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:RCAP_rcc01447
OrganismRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) [Complete proteome] [HAMAP]
Taxonomic identifier272942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Pyridoxal phosphate. Ref.4

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.

Ontologies

Keywords
   Biological processHeme biosynthesis
   LigandPyridoxal phosphate
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Complete 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_0000163828

Sites

Active site2481 Ref.4
Binding site211Substrate
Binding site1371Substrate
Binding site1561Substrate
Binding site1891Pyridoxal phosphate
Binding site2171Pyridoxal phosphate
Binding site2451Pyridoxal phosphate
Binding site2771Pyridoxal phosphate
Binding site2781Pyridoxal phosphate
Binding site3651Substrate

Amino acid modifications

Modified residue2481N6-(pyridoxal phosphate)lysine Probable

Experimental info

Sequence conflict1281V → L in CAA37857. Ref.1
Sequence conflict1281V → L in CAA37393. Ref.2
Sequence conflict402 – 4098Missing in CAA37857. Ref.1
Sequence conflict402 – 4098Missing in CAA37393. Ref.2

Secondary structure

................................................................... 409
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18079 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: FCC89DA6EBA8DFB3

FASTA40944,374
        10         20         30         40         50         60 
MDYNLALDKA IQKLHDEGRY RTFIDIEREK GAFPKAQWNR PDGGKQDITV WCGNDYLGMG 

        70         80         90        100        110        120 
QHPVVLAAMH EALEAVGAGS GGTRNISGTT AYHRRLEAEI ADLHGKEAAL VFSSAYIAND 

       130        140        150        160        170        180 
ATLSTLRVLF PGLIIYSDSL NHASMIEGIK RNAGPKRIFR HNDVAHLREL IAADDPAAPK 

       190        200        210        220        230        240 
LIAFESVYSM DGDFGPIKEI CDIADEFGAL TYIDEVHAVG MYGPRGAGVA ERDGLMHRID 

       250        260        270        280        290        300 
IFNGTLAKAY GVFGGYIAAS AKMVDAVRSY APGFIFSTSL PPAIAAGAQA SIAFLKTAEG 

       310        320        330        340        350        360 
QKLRDAQQMH AKVLKMRLKA LGMPIIDHGS HIVPVVIGDP VHTKAVSDML LSDYGVYVQP 

       370        380        390        400 
INFPTVPRGT ERLRFTPSPV HDLKQIDGLV HAMDLLWARC ALNRAEASA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the hemA gene of Rhodobacter capsulatus and isolation of a delta-aminolevulinic acid-dependent mutant strain."
Hornberger U., Liebetanz R., Tichy H.V., Drews G.
Mol. Gen. Genet. 221:371-378(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[2]"Use of a lacZ fusion to study transcriptional regulation of the Rhodobacter capsulatus hemA gene."
Wright M.S., Eckert J.J., Biel S.W., Biel A.J.
FEMS Microbiol. Lett. 62:339-342(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[3]"Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003."
Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R.
J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
[4]"Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans."
Astner I., Schulze J.O., van den Heuvel J., Jahn D., Schubert W.D., Heinz D.W.
EMBO J. 24:3166-3177(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-401, SUBUNIT, COFACTOR-BINDING SITES, SUBSTRATE-BINDING SITES, ACTIVE SITE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53309 Genomic DNA. Translation: CAA37393.1.
X53864 Genomic DNA. Translation: CAA37857.1.
CP001312 Genomic DNA. Translation: ADE85192.1.
PIRS10528.
RefSeqYP_003577599.1. NC_014034.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BWNX-ray2.10A/B/D/E1-401[»]
2BWOX-ray2.80A/B/D/E1-401[»]
2BWPX-ray2.70A/B/D/E1-401[»]
ProteinModelPortalP18079.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE85192; ADE85192; RCAP_rcc01447.
GeneID9004270.
KEGGrcp:RCAP_rcc01447.
PATRIC35502998. VBIRhoCap134200_1459.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000221020.
KOK00643.
OMATEGRYRT.

Enzyme and pathway databases

BioCycRCAP272942:GJIY-1471-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...

Other

EvolutionaryTraceP18079.

Entry information

Entry nameHEM1_RHOCB
AccessionPrimary (citable) accession number: P18079
Secondary accession number(s): D5AT85
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 31, 2011
Last modified: October 16, 2013
This is version 100 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways