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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Xanthomonas campestris pv. phaseoli
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), 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

Keywordsi

Molecular functionIsomerase
Biological processPorphyrin biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase (EC:5.4.3.8)
Short name:
GSA
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name:
GSA-AT
Gene namesi
Name:hemL
OrganismiXanthomonas campestris pv. phaseoli
Taxonomic identifieri317013 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001204701 – 429Glutamate-1-semialdehyde 2,1-aminomutaseAdd BLAST429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei267N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PRIDEiQ06741

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ06741
SMRiQ06741
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

CDDicd00610 OAT_like, 1 hit
Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_00375 HemL_aminotrans_3, 1 hit
InterProiView protein in InterPro
IPR004639 4pyrrol_synth_GluAld_NH2Trfase
IPR005814 Aminotrans_3
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00202 Aminotran_3, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR00713 hemL, 1 hit
PROSITEiView protein in PROSITE
PS00600 AA_TRANSFER_CLASS_3, 1 hit

Sequencei

Sequence statusi: Complete.

Q06741-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNHSRSHALF AQAQTLLPGG VNSPVRAFKS VGGEPFFVAR ADGPYLFDVD
60 70 80 90 100
DNRYIDYVGS WGPMIAGHNH PAVREAVEQS IRNGLSFGAP CAAEVTMAQT
110 120 130 140 150
IARLVPSCEM VRMVNSGTEA TLSAVRLARG ATGRNRIIKF EGCYHGHGDS
160 170 180 190 200
FLVKAGSGML TLGVPTSPGV PAGLSELTAT LSFNDFEGAT ALFDEIGAEV
210 220 230 240 250
AAVIIEPVVG NANCIPPQAG YLQHLRTLCT RHGALLIFDE VMTGFRVALG
260 270 280 290 300
GAQAHYGVTP DLTTFGKIIG GGMPVGAYGG RRDLMEQVAP AGPIYQAGTL
310 320 330 340 350
SGNPVAMAAG LAMLELVQEP GFHTRLSEAT SMLCEGLEDA ARAAGIAVTT
360 370 380 390 400
NQVGGMFGLF FTDDVVESYA QATACDITSF NRFFHAMLQR GVYLAPSAYE
410 420
AGFMSSAHDE AVIEATLAAA REAFADVAR
Length:429
Mass (Da):45,044
Last modified:June 1, 1994 - v1
Checksum:iC134A4589BCDD700
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12642 Genomic DNA Translation: BAA02163.1
PIRiA48377
RefSeqiWP_022558547.1, NZ_LT960913.1

Genome annotation databases

GeneIDi34207860

Similar proteinsi

Entry informationi

Entry nameiGSA_XANCH
AccessioniPrimary (citable) accession number: Q06741
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 23, 2018
This is version 100 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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