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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

GO - Molecular functioni

  1. glutamate-1-semialdehyde 2,1-aminomutase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: InterPro
  3. transaminase activity Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciSSP321327:GHFX-2378-MONOMER.
UniPathwayiUPA00251; UER00317.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSAUniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferaseUniRule annotation
Short name:
GSA-ATUniRule annotation
Gene namesi
Name:hemLUniRule annotation
Ordered Locus Names:CYA_2386
OrganismiSynechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime)
Taxonomic identifieri321327 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000008818: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000243630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei276 – 2761N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiQ2JS70.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi321327.CYA_2386.

Structurei

3D structure databases

ProteinModelPortaliQ2JS70.
SMRiQ2JS70. Positions 10-436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2JS70-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSTLPTRSF NTSRSRQIFA RAQQLMPGGV SSPVRAFKSV GGDPVVFDRV
60 70 80 90 100
AGAYAWDVDG NQYIDYIGSW GPAIVGHAHP EVIEALRRAL EKGTSFGAPC
110 120 130 140 150
VLENELAERV IEAVPSVEMV RFVNSGTEAC MAALRLMRAY TGREKVIKFE
160 170 180 190 200
GCYHGHADMF LVKAGSGVAT LGLPDSPGVP KAATSATLTA PYNDLEAVKA
210 220 230 240 250
LFEQYPDSIA GVILEPVVGN AGFIPPQPGF LEGLRELTQK YGALLVFDEV
260 270 280 290 300
MTGFRISYGG VQAKFGVIPD LTTLGKVIGG GLPVGAYGGR REIMEMVAPA
310 320 330 340 350
GPMYQAGTLS GNPLAMTAGI HTLDILRRPG TYEYLERITE QLATGLLQIA
360 370 380 390 400
QETGHEMCGG YLPGMFGFFF TAGPVRNYEE AKRSDLQKFA RFHRGMLERG
410 420 430
VYLAPSQFEA GFTSLAHTEA DVERTLEAAR EVLRTL
Length:436
Mass (Da):47,014
Last modified:March 7, 2006 - v1
Checksum:iCA535217113EF667
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000239 Genomic DNA. Translation: ABD00512.1.
RefSeqiWP_011431185.1. NC_007775.1.
YP_475775.1. NC_007775.1.

Genome annotation databases

EnsemblBacteriaiABD00512; ABD00512; CYA_2386.
GeneIDi3898472.
KEGGicya:CYA_2386.
PATRICi23813034. VBISynSp90045_2344.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000239 Genomic DNA. Translation: ABD00512.1.
RefSeqiWP_011431185.1. NC_007775.1.
YP_475775.1. NC_007775.1.

3D structure databases

ProteinModelPortaliQ2JS70.
SMRiQ2JS70. Positions 10-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi321327.CYA_2386.

Proteomic databases

PRIDEiQ2JS70.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD00512; ABD00512; CYA_2386.
GeneIDi3898472.
KEGGicya:CYA_2386.
PATRICi23813034. VBISynSp90045_2344.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.
BioCyciSSP321327:GHFX-2378-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
    Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
    ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JA-3-3Ab.

Entry informationi

Entry nameiGSA_SYNJA
AccessioniPrimary (citable) accession number: Q2JS70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 7, 2006
Last modified: January 7, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete 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.