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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
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 / PAO1 / 1C / PRS 101 / LMG 12228)
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120433Add
BLAST

Amino acid modifications

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

Proteomic databases

PaxDbiP48247.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi208964.PA3977.

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Turni12 – 143Combined sources
Helixi16 – 183Combined sources
Helixi22 – 254Combined sources
Turni27 – 293Combined sources
Beta strandi36 – 416Combined sources
Beta strandi43 – 464Combined sources
Beta strandi51 – 566Combined sources
Helixi57 – 593Combined sources
Helixi69 – 7911Combined sources
Helixi90 – 10213Combined sources
Beta strandi107 – 1137Combined sources
Helixi115 – 13016Combined sources
Beta strandi134 – 1396Combined sources
Helixi147 – 1493Combined sources
Beta strandi150 – 1534Combined sources
Beta strandi161 – 1655Combined sources
Helixi170 – 1734Combined sources
Beta strandi176 – 1805Combined sources
Helixi184 – 19411Combined sources
Helixi195 – 1973Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi209 – 2113Combined sources
Helixi219 – 23012Combined sources
Beta strandi233 – 2375Combined sources
Turni239 – 2446Combined sources
Helixi249 – 2546Combined sources
Beta strandi259 – 2646Combined sources
Helixi265 – 2684Combined sources
Beta strandi274 – 2785Combined sources
Helixi280 – 2834Combined sources
Turni287 – 2893Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi295 – 2973Combined sources
Helixi302 – 31413Combined sources
Helixi320 – 34122Combined sources
Beta strandi347 – 3515Combined sources
Beta strandi354 – 3585Combined sources
Helixi368 – 3736Combined sources
Helixi376 – 38813Combined sources
Helixi409 – 42416Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5I92X-ray1.75A/B/C/D/E/F1-427[»]
ProteinModelPortaliP48247.
SMRiP48247. Positions 1-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
InParanoidiP48247.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.
PhylomeDBiP48247.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571A → S in CAA57575 (PubMed:7565600).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
5I92X-ray1.75A/B/C/D/E/F1-427[»]
ProteinModelPortaliP48247.
SMRiP48247. Positions 1-426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3977.

Proteomic databases

PaxDbiP48247.

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.
OrthoDBiEOG6QVRHN.
PhylomeDBiP48247.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.

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

« Hide 'large scale' publications
  1. "Cloning, mapping and characterization of the Pseudomonas aeruginosa hemL gene."
    Hungerer C., Troup B., Romling U., Jahn D.
    Mol. Gen. Genet. 248:375-380(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

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: June 8, 2016
This is version 121 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.