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Protein

5-aminolevulinate synthase

Gene

hemA

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211SubstrateBy similarity
Binding sitei136 – 1361SubstrateBy similarity
Binding sitei188 – 1881Pyridoxal phosphateBy similarity
Binding sitei216 – 2161Pyridoxal phosphateBy similarity
Binding sitei244 – 2441Pyridoxal phosphateBy similarity
Active sitei247 – 2471By similarity
Binding sitei276 – 2761Pyridoxal phosphateBy similarity
Binding sitei277 – 2771Pyridoxal phosphateBy similarity
Binding sitei362 – 3621SubstrateBy similarity

GO - Molecular functioni

  1. 5-aminolevulinate synthase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciBJAP224911:GJEJ-1210-MONOMER.
UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase (EC:2.3.1.37)
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene namesi
Name:hemA
Ordered Locus Names:bll1200
OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Taxonomic identifieri224911 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
ProteomesiUP000002526 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4094095-aminolevulinate synthasePRO_0000163825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei247 – 2471N6-(pyridoxal phosphate)lysineCurated

Interactioni

Protein-protein interaction databases

STRINGi224911.bll1200.

Structurei

3D structure databases

ProteinModelPortaliP08262.
SMRiP08262. Positions 2-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221020.
InParanoidiP08262.
KOiK00643.
OrthoDBiEOG6Q8HZD.
PhylomeDBiP08262.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 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]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08262-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYSQFFNSA LDRLHTERRY RVFADLERMA GRFPHAIWHS PKGKRDVVIW
60 70 80 90 100
CSNDYLGMGQ HPKVVGAMVE TATRVGTGAG GTRNIAGTHH PLVQLEAELA
110 120 130 140 150
DLHGKEAALL FTSGYVSNQT GIATIAKLIP NCLILSDELN HNSMIEGIRQ
160 170 180 190 200
SGCERQVFRH NDLADLEALL KAAGANRPKL IACESLYSMD GDVAPLAKIC
210 220 230 240 250
DLAEKYNAMT YVDEVHAVGM YGPRGGGIAE RDGVMHRIDI LEGTLAKAFG
260 270 280 290 300
CLGGYIAANG QIIDAVRSYA PGFIFTTALP PAICSAATAA IKHLKTSSWE
310 320 330 340 350
RERHQDRAAR VKAILNAAGL PVMSSDTHIV PLFIGDAEKC KQASDLLLEE
360 370 380 390 400
HGIYIQPINY PTVAKGSERL RITPSPYHDD GLIDQLAEAL LQVWDRLGLP

LKQKSLAAE
Length:409
Mass (Da):44,574
Last modified:February 28, 2003 - v2
Checksum:iB21B011EB9542D66
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2611Q → R in AAA26216 (PubMed:3609750).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16751 Genomic DNA. Translation: AAA26216.1.
BA000040 Genomic DNA. Translation: BAC46465.1.
PIRiA27478. SYZJAL.
RefSeqiNP_767840.1. NC_004463.1.

Genome annotation databases

EnsemblBacteriaiBAC46465; BAC46465; BAC46465.
GeneIDi1049580.
KEGGibja:bll1200.
PATRICi21185942. VBIBraJap65052_1241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16751 Genomic DNA. Translation: AAA26216.1.
BA000040 Genomic DNA. Translation: BAC46465.1.
PIRiA27478. SYZJAL.
RefSeqiNP_767840.1. NC_004463.1.

3D structure databases

ProteinModelPortaliP08262.
SMRiP08262. Positions 2-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224911.bll1200.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC46465; BAC46465; BAC46465.
GeneIDi1049580.
KEGGibja:bll1200.
PATRICi21185942. VBIBraJap65052_1241.

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221020.
InParanoidiP08262.
KOiK00643.
OrthoDBiEOG6Q8HZD.
PhylomeDBiP08262.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.
BioCyciBJAP224911:GJEJ-1210-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 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]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the Bradyrhizobium japonicum gene hemA encoding 5-aminolevulinic acid synthase."
    McClung C.R., Somerville J.E., Guerinot M.L., Chelm B.K.
    Gene 54:133-139(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Entry informationi

Entry nameiHEM1_BRADU
AccessioniPrimary (citable) accession number: P08262
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 28, 2003
Last modified: January 7, 2015
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.