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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT)
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. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciHDEF572265:GJAB-1741-MONOMER.
UniPathwayiUPA00251; UER00317.

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:HDEF_1725
OrganismiHamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT)
Taxonomic identifieri572265 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeaphid secondary symbiontsCandidatus Hamiltonella
ProteomesiUP000002334 Componenti: Chromosome

Subcellular locationi

  1. 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 – 428428Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000382321Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiC4K6Y5.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi572265.HDEF_1725.

Structurei

3D structure databases

ProteinModelPortaliC4K6Y5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0001.
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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C4K6Y5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDSNKLYDL AQCFIPGGVN SPVRAFQGVD GKPFFVEKAG GAYLYDVDGR
60 70 80 90 100
AYIDYVGSWG PMILGHRHPV ICDALTKAIE NGISFGAPTE IEVKMAQLLT
110 120 130 140 150
QLMPSMDMVR MVNSGTEATM SAIRLARGFT KRDKIIKFEG CYHGHSDCLL
160 170 180 190 200
VKAGSGALTL GQADSPGVPK DFAQHTLICT YNDLSSVRKN LEDYPKEVAA
210 220 230 240 250
IIVEPVAGNM NCILPSENFL PGLRQLCDEF GALLIMDEVM TGFRVALGGA
260 270 280 290 300
QEYYNIKPDL TCLGKIIGGG MPVAAFGGRK EVMSILAPLG PVYQAETLSG
310 320 330 340 350
HPLGMAAGFA CLTELARPGL HKKLTELTTL LVLNLKKAAQ EHNIPLIINH
360 370 380 390 400
LGGMFGFFFT DAKTVTCYED VKKCNIERFK RFFYFMLKEG IYFAPSAFEA
410 420
GFMSLAHGVE EIEKTISSAR RCFAQSRF
Length:428
Mass (Da):46,751
Last modified:July 7, 2009 - v1
Checksum:i2AC9AB5ECBA0E355
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001277 Genomic DNA. Translation: ACQ68328.1.
RefSeqiYP_002924476.1. NC_012751.1.

Genome annotation databases

EnsemblBacteriaiACQ68328; ACQ68328; HDEF_1725.
KEGGihde:HDEF_1725.
PATRICi31974909. VBICanHam112931_1715.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001277 Genomic DNA. Translation: ACQ68328.1.
RefSeqiYP_002924476.1. NC_012751.1.

3D structure databases

ProteinModelPortaliC4K6Y5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi572265.HDEF_1725.

Proteomic databases

PRIDEiC4K6Y5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACQ68328; ACQ68328; HDEF_1725.
KEGGihde:HDEF_1725.
PATRICi31974909. VBICanHam112931_1715.

Phylogenomic databases

eggNOGiCOG0001.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciHDEF572265:GJAB-1741-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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Hamiltonella defensa, genome evolution of protective bacterial endosymbiont from pathogenic ancestors."
    Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.
    Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 5AT.

Entry informationi

Entry nameiGSA_HAMD5
AccessioniPrimary (citable) accession number: C4K6Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: July 7, 2009
Last modified: April 29, 2015
This is version 44 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, 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.