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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Alteromonas macleodii (strain DSM 17117 / Deep ecotype)
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: protoporphyrin-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

BioCyciAMAC314275:GHA7-503-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:MADE_1002445
OrganismiAlteromonas macleodii (strain DSM 17117 / Deep ecotype)
Taxonomic identifieri314275 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas
ProteomesiUP000001870 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 – 426426Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000382249Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiB4S0D0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi314275.MADE_1002445.

Structurei

3D structure databases

ProteinModelPortaliB4S0D0.
SMRiB4S0D0. Positions 2-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0001.
KOiK01845.

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.

B4S0D0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKSEALFTR AQKTIPGGVN SPVRAFKAVG GTPRFITKAD GAYMWDADGK
60 70 80 90 100
QYIDYIQSWG PMILGHNNAP IREAVIEASC SGLSFGAPTE AEVIMAELVS
110 120 130 140 150
EMVPSMEMVR MVNSGTEATM SAIRLARGYT SRNKIVKFEG CYHGHADSLL
160 170 180 190 200
VKAGSGALTL GVPSSPGVPA NVAEHTLTVE FNNLDSVKEI FETHGDDIAC
210 220 230 240 250
IIVEPVAGNM NCIPPVEGFL EGLRAICDQY GSVLIFDEVM TGFRVSRGGA
260 270 280 290 300
QERFNVKPDL TCLGKVIGGG MPVGCFGGRR DIITHIAPTG PVYQAGTLSG
310 320 330 340 350
NPVAMAAGLA ALTQIKQPGL YDSIFENTQA LVDGFQDLAD KHNISLTTNI
360 370 380 390 400
AGSMFGIFFT DVEKVTNYKQ AINCNTEQFN KFYHGMLEQG VYLAPASYEA
410 420
GFVSKAHDAE VIEKTLAAAD KVFSTL
Length:426
Mass (Da):45,574
Last modified:September 1, 2009 - v2
Checksum:iD7DA4CD274FB9C55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001103 Genomic DNA. Translation: AEA96638.1.
RefSeqiWP_012516993.1. NC_011138.3.
YP_004425636.1. NC_011138.3.

Genome annotation databases

EnsemblBacteriaiAEA96638; AEA96638; MADE_1002445.
GeneIDi10555833.
KEGGiamc:MADE_1002445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001103 Genomic DNA. Translation: AEA96638.1.
RefSeqiWP_012516993.1. NC_011138.3.
YP_004425636.1. NC_011138.3.

3D structure databases

ProteinModelPortaliB4S0D0.
SMRiB4S0D0. Positions 2-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi314275.MADE_1002445.

Proteomic databases

PRIDEiB4S0D0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAEA96638; AEA96638; MADE_1002445.
GeneIDi10555833.
KEGGiamc:MADE_1002445.

Phylogenomic databases

eggNOGiCOG0001.
KOiK01845.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciAMAC314275:GHA7-503-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. "Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
    Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
    ISME J. 2:1194-1212(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17117 / Deep ecotype.

Entry informationi

Entry nameiGSA_ALTMD
AccessioniPrimary (citable) accession number: B4S0D0
Secondary accession number(s): F2G6G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 1, 2009
Last modified: June 24, 2015
This is version 56 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

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.