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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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)
  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

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
Ordered Locus Names:PA3977
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3977.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001204331 – 427Glutamate-1-semialdehyde 2,1-aminomutaseAdd BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei265N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PaxDbiP48247.
PRIDEiP48247.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi208964.PA3977.

Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 11Combined sources9
Turni12 – 14Combined sources3
Helixi16 – 18Combined sources3
Helixi22 – 25Combined sources4
Turni27 – 29Combined sources3
Beta strandi36 – 41Combined sources6
Beta strandi43 – 46Combined sources4
Beta strandi51 – 56Combined sources6
Helixi57 – 59Combined sources3
Helixi69 – 79Combined sources11
Helixi90 – 102Combined sources13
Beta strandi107 – 113Combined sources7
Helixi115 – 130Combined sources16
Beta strandi134 – 139Combined sources6
Helixi147 – 149Combined sources3
Beta strandi150 – 153Combined sources4
Beta strandi161 – 165Combined sources5
Helixi170 – 173Combined sources4
Beta strandi176 – 180Combined sources5
Helixi184 – 194Combined sources11
Helixi195 – 197Combined sources3
Beta strandi198 – 203Combined sources6
Beta strandi205 – 207Combined sources3
Beta strandi209 – 211Combined sources3
Helixi219 – 230Combined sources12
Beta strandi233 – 237Combined sources5
Turni239 – 244Combined sources6
Helixi249 – 254Combined sources6
Beta strandi259 – 264Combined sources6
Helixi265 – 268Combined sources4
Beta strandi274 – 278Combined sources5
Helixi280 – 283Combined sources4
Turni287 – 289Combined sources3
Beta strandi290 – 292Combined sources3
Beta strandi295 – 297Combined sources3
Helixi302 – 314Combined sources13
Helixi320 – 341Combined sources22
Beta strandi347 – 351Combined sources5
Beta strandi354 – 358Combined sources5
Helixi368 – 373Combined sources6
Helixi376 – 388Combined sources13
Helixi409 – 424Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5I92X-ray1.75A/B/C/D/E/F1-427[»]
ProteinModelPortaliP48247.
SMRiP48247.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
InParanoidiP48247.
KOiK01845.
OMAiCGHAHPE.
PhylomeDBiP48247.

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.
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.

P48247-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRSETLFNN AQKHIPGGVN SPVRAFKSVG GTPLFFKHAE GAYVLDEDDK
60 70 80 90 100
RYVDYVGSWG PMILGHSHPD VLDAVRRQLD HGLSYGAPTA LEVEMADLVC
110 120 130 140 150
SMVPSMEMVR MVSSGTEATM SAIRLARGYT GRDSIIKFEG CYHGHSDSLL
160 170 180 190 200
VKAGSGALTF GVPNSPGVPA AFAKHTLTLP FNDIEAVRKT LGEVGKEVAC
210 220 230 240 250
IIVEPVAGNM NCVPPAPGFL EGLREACDEH GVVLIFDEVM TGFRVALGGA
260 270 280 290 300
QAYYGVTPDL STFGKIIGGG MPVGAFGGKR EIMQQISPLG PVYQAGTLSG
310 320 330 340 350
NPLAMAAGLT TLRLISRPGF HDELTAYTTR MLDGLQQRAD AAGIPFVTTQ
360 370 380 390 400
AGGMFGLYFS GADAIVTFED VMASDVERFK RFFHLMLDGG VYLAPSAFEA
410 420
GFTSIAHGDK ELEITLNAAE KAFAALK
Length:427
Mass (Da):45,398
Last modified:December 8, 2000 - v2
Checksum:i670EB87D144E2D28
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti157A → S in CAA57575 (PubMed:7565600).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82072 Genomic DNA. Translation: CAA57575.1.
AE004091 Genomic DNA. Translation: AAG07364.1.
PIRiG83149.
S57898.
RefSeqiNP_252666.1. NC_002516.2.
WP_003093150.1. NZ_ASJY01000635.1.

Genome annotation databases

EnsemblBacteriaiAAG07364; AAG07364; PA3977.
GeneIDi880859.
KEGGipae:PA3977.
PATRICi19842625. VBIPseAer58763_4169.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82072 Genomic DNA. Translation: CAA57575.1.
AE004091 Genomic DNA. Translation: AAG07364.1.
PIRiG83149.
S57898.
RefSeqiNP_252666.1. NC_002516.2.
WP_003093150.1. NZ_ASJY01000635.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5I92X-ray1.75A/B/C/D/E/F1-427[»]
ProteinModelPortaliP48247.
SMRiP48247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3977.

Proteomic databases

PaxDbiP48247.
PRIDEiP48247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07364; AAG07364; PA3977.
GeneIDi880859.
KEGGipae:PA3977.
PATRICi19842625. VBIPseAer58763_4169.

Organism-specific databases

PseudoCAPiPA3977.

Phylogenomic databases

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
InParanoidiP48247.
KOiK01845.
OMAiCGHAHPE.
PhylomeDBiP48247.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.

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.
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...

Entry informationi

Entry nameiGSA_PSEAE
AccessioniPrimary (citable) accession number: P48247
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 8, 2000
Last modified: November 2, 2016
This is version 124 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.