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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
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

Pathwayi

GO - Molecular functioni

  1. glutamate-1-semialdehyde 2,1-aminomutase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: InterPro
  3. transaminase activity Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciGMET269799:GHNY-3404-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:Gmet_3356
OrganismiGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
Taxonomic identifieri269799 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter
ProteomesiUP000007073 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000243575Add
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

STRINGi269799.Gmet_3356.

Structurei

3D structure databases

ProteinModelPortaliQ39QA6.
SMRiQ39QA6. Positions 1-419.
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.
OMAiTNFDEAK.
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.

Q39QA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTSHSKELF AKAQEIIPGG VNSPVRAFKS VGAEPVFIKK ASGSTIIDAD
60 70 80 90 100
DNAYIDYVGS WGPMILGHCH PRIVASVQRA TENGSSFGAP TELEITLAEM
110 120 130 140 150
VVAAVPSIEM VRMVSSGTEA TMSAIRLARG YTGRDKIIKF SGCYHGHADS
160 170 180 190 200
LLVKAGSGAA TFGVPDSPGV PRDFAQHTLT ATFNDLESVE ELICAHSREV
210 220 230 240 250
ACIIVEPIAG NMGTVPPRAG FLEGLREICT NEGIILIFDE VMTGFRVAYG
260 270 280 290 300
GAQERYGITP DMTTLGKIIG GGLPVGAFGG KREIMQQLSP SGGVYQAGTL
310 320 330 340 350
SGNPLAMTAG IETLKLLQED GFYGRLEEKS RALAEGIADA ARRAGYPIYS
360 370 380 390 400
TRVGSMFCAF FTNGEVHDWT SAAMCDTKSF ATFFRSMLEE GIYLAPSQFE
410 420
TAFVSIAHSS EDIEKTIAAA FSCFKKL
Length:427
Mass (Da):45,479
Last modified:November 22, 2005 - v1
Checksum:i0EEF1BBE815FB266
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000148 Genomic DNA. Translation: ABB33568.1.
RefSeqiYP_006722310.1. NC_007517.1.

Genome annotation databases

EnsemblBacteriaiABB33568; ABB33568; Gmet_3356.
KEGGigme:Gmet_3356.
PATRICi22005988. VBIGeoMet55070_3397.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000148 Genomic DNA. Translation: ABB33568.1.
RefSeqiYP_006722310.1. NC_007517.1.

3D structure databases

ProteinModelPortaliQ39QA6.
SMRiQ39QA6. Positions 1-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269799.Gmet_3356.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB33568; ABB33568; Gmet_3356.
KEGGigme:Gmet_3356.
PATRICi22005988. VBIGeoMet55070_3397.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiTNFDEAK.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciGMET269799:GHNY-3404-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. "Complete sequence of Geobacter metallireducens GS-15."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GS-15 / ATCC 53774 / DSM 7210.

Entry informationi

Entry nameiGSA_GEOMG
AccessioniPrimary (citable) accession number: Q39QA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 22, 2005
Last modified: April 1, 2015
This is version 73 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.