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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Serratia proteamaculans (strain 568)
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

Pathway:iprotoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciSPRO399741:GI55-809-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:Spro_0781
OrganismiSerratia proteamaculans (strain 568)
Taxonomic identifieri399741 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia
ProteomesiUP000007074 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000382368Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei268 – 2681N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiA8G9U7.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi399741.Spro_0781.

Structurei

3D structure databases

ProteinModelPortaliA8G9U7.
SMRiA8G9U7. Positions 4-424.
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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A8G9U7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLHSKSESL YAQAKQVIPG GVNSPVRAFN GVGGVPLFIE RADGAYLFDV
60 70 80 90 100
DGKAYIDYVG SWGPMVLGHN HPAIRNAVIE AAQRGLSFGA PTEMEVKMAE
110 120 130 140 150
LVTELVPTMD MVRMVNSGTE ATMSAIRLAR GYTNRDKIIK FEGCYHGHAD
160 170 180 190 200
CLLVKAGSGA LTLGQPNSPG VPADFAKHTL TCTFNDLDSV RTAFEQYPSE
210 220 230 240 250
IACIIVEPVA GNMNCVPPLP EFLPGLRALC DKYGALLIID EVMTGFRVAL
260 270 280 290 300
AGAQSYYDVV PDLTCLGKII GGGMPVGAFG GRREVMAALA PTGPVYQAGT
310 320 330 340 350
LSGNPIAMAA GFACLTEVSQ VGVHQTLTEL TDMLAAGLLH AAKEENVALV
360 370 380 390 400
VNHVGGMFGL FFTDALSVTS YQDVMQCDVE RFKRFFHLML EEGVYLAPSA
410 420
FEAGFMSIAH SKEDIQRTID AARRCFAKL
Length:429
Mass (Da):45,872
Last modified:November 13, 2007 - v1
Checksum:iBB5C6F7785111933
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000826 Genomic DNA. Translation: ABV39887.1.
RefSeqiWP_012005229.1. NC_009832.1.

Genome annotation databases

EnsemblBacteriaiABV39887; ABV39887; Spro_0781.
KEGGispe:Spro_0781.
PATRICi32414206. VBISerPro44537_0810.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000826 Genomic DNA. Translation: ABV39887.1.
RefSeqiWP_012005229.1. NC_009832.1.

3D structure databases

ProteinModelPortaliA8G9U7.
SMRiA8G9U7. Positions 4-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi399741.Spro_0781.

Proteomic databases

PRIDEiA8G9U7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV39887; ABV39887; Spro_0781.
KEGGispe:Spro_0781.
PATRICi32414206. VBISerPro44537_0810.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciSPRO399741:GI55-809-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 568.

Entry informationi

Entry nameiGSA_SERP5
AccessioniPrimary (citable) accession number: A8G9U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: November 13, 2007
Last modified: July 22, 2015
This is version 61 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.