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Q04512 (HEM1_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. 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 1
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:RHOS4_15770
ORF Names:RSP_2984
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Reference proteome] [HAMAP]
Taxonomic identifier272943 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter ›

Protein attributes

Sequence length407 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.

Ontologies

Keywords
   Biological processHeme biosynthesis
   LigandPyridoxal phosphate
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference 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: 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 – 4074075-aminolevulinate synthase 1
PRO_0000163829

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 site3631Substrate By similarity

Amino acid modifications

Modified residue2481N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04512 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: DCDE2484BFACC7F0

FASTA40744,616
        10         20         30         40         50         60 
MDYNLALDTA LNRLHTEGRY RTFIDIERRK GAFPKAMWRK PDGSEKEITV WCGNDYLGMG 

        70         80         90        100        110        120 
QHPVVLGAMH EALDSTGAGS GGTRNISGTT LYHKRLEAEL ADLHGKEAAL VFSSAYIAND 

       130        140        150        160        170        180 
ATLSTLPQLI PGLVIVSDKL NHASMIEGIR RSGTEKHIFK HNDLDDLRRI LTSIGKDRPI 

       190        200        210        220        230        240 
LVAFESVYSM DGDFGRIEEI CDIADEFGAL KYIDEVHAVG MYGPRGGGVA ERDGLMDRID 

       250        260        270        280        290        300 
IINGTLGKAY GVFGGYIAAS SKMCDAVRSY APGFIFSTSL PPVVAAGAAA SVRHLKGDVE 

       310        320        330        340        350        360 
LREKHQTQAR ILKMRLKGLG LPIIDHGSHI VPVHVGDPVH CKMISDMLLE HFGIYVQPIN 

       370        380        390        400 
FPTVPRGTER LRFTPSPVHD SGMIDHLVKA MDVLWQHCAL NRAEVVA

« Hide

References

« Hide 'large scale' references
[1]"Expression of the Rhodobacter sphaeroides hemA and hemT genes, encoding two 5-aminolevulinic acid synthase isozymes."
Neidle E.L., Kaplan S.
J. Bacteriol. 175:2292-2303(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L07490 Genomic DNA. Translation: AAA72325.1.
CP000143 Genomic DNA. Translation: ABA79145.1.
RefSeqYP_353046.1. NC_007493.1.

3D structure databases

ProteinModelPortalQ04512.
SMRQ04512. Positions 1-395.
ModBaseSearch...

Protein-protein interaction databases

STRING272943.RSP_2984.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3720398.
KEGGrsp:RSP_2984.
PATRIC23153077. VBIRhoSph57909_1924.

Phylogenomic databases

eggNOGCOG0156.
HOGENOMHOG000221020.
KOK00643.
OMAICDIADE.
ProtClustDBPRK09064.

Enzyme and pathway databases

BioCycRSPH272943:GJAS-1613-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. 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_RHOS4
AccessionPrimary (citable) accession number: Q04512
Secondary accession number(s): Q3J239
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 1, 2013
This is version 87 of the entry and version 1 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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