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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Stenotrophomonas maltophilia (strain K279a)
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

BioCyciSMAL522373:GJE8-3746-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:Smlt3873
OrganismiStenotrophomonas maltophilia (strain K279a)
Taxonomic identifieri522373 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
ProteomesiUP000008840 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_1000121926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei267 – 2671N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi522373.Smlt3873.

Structurei

3D structure databases

ProteinModelPortaliB2FT35.
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.

B2FT35-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNHDQSHALF SRAQQLLPGG VNSPVRAFKS VGGEPFFVER ADGAYLYDVD
60 70 80 90 100
GNRYIDYVGS WGPMIVGHNH PAVRQAVKKA IDNGLSFGAP CAGEVTMAET
110 120 130 140 150
ITRLVPSCEM VRMVNSGTEA TLSAIRLARG ATGRNRIVKF EGCYHGHGDS
160 170 180 190 200
FLVKAGSGML TLGVPTSPGV PAGLSELTLT LPYNDFEAAT ALFEQQGDDI
210 220 230 240 250
AGLIIEPVVG NANCIPPREG YLQHLRALCT KHGALLIFDE VMTGFRVALG
260 270 280 290 300
GAQAHYGITP DLTTFGKIIG GGMPVGAYGG RRELMQQIAP AGPIYQAGTL
310 320 330 340 350
SGNPVAMAAG LAMLELVQQP GFHADLAERT ARLCAGLEAA AADAGVAVTT
360 370 380 390 400
TRVGAMFGLF FTSEKVETYA QATACDIPAF NRFFHAMLEQ GVFLAPSAYE
410 420
AGFLSSAHDD AVIEATLAAA RVAFRAAKG
Length:429
Mass (Da):45,067
Last modified:June 10, 2008 - v1
Checksum:i62C75E93A51E934A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM743169 Genomic DNA. Translation: CAQ47277.1.
RefSeqiWP_012481173.1. NC_010943.1.

Genome annotation databases

EnsemblBacteriaiCAQ47277; CAQ47277; Smlt3873.
GeneIDi6394738.
KEGGisml:Smlt3873.
PATRICi23703197. VBISteMal45202_3648.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM743169 Genomic DNA. Translation: CAQ47277.1.
RefSeqiWP_012481173.1. NC_010943.1.

3D structure databases

ProteinModelPortaliB2FT35.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi522373.Smlt3873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAQ47277; CAQ47277; Smlt3873.
GeneIDi6394738.
KEGGisml:Smlt3873.
PATRICi23703197. VBISteMal45202_3648.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciSMAL522373:GJE8-3746-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. "The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
    Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A.
    , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
    Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K279a.

Entry informationi

Entry nameiGSA_STRMK
AccessioniPrimary (citable) accession number: B2FT35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: July 22, 2015
This is version 56 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.