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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Mycobacterium sp. (strain JLS)
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

BioCyciMSP164757:GHV3-687-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:Mjls_0683
OrganismiMycobacterium sp. (strain JLS)
Taxonomic identifieri164757 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000002152: Chromosome

Subcellular locationi

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 – 438438Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000382347Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiA3PUB7.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi164757.Mjls_0683.

Structurei

3D structure databases

ProteinModelPortaliA3PUB7.
SMRiA3PUB7. Positions 8-425.
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]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A3PUB7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAHHTATEQ SARLFADACA VIPGGVNSPV RAFNAVGGTP RFITSANGYW
60 70 80 90 100
LTDADDNRYV DLVCSWGPMI LGHAHPAVVE AVQRVAADGL SFGAPTPSET
110 120 130 140 150
ELASEIISRV APVERLRMVN SGTEATMSAI RLARGFTGRP KIVKFSGCYH
160 170 180 190 200
GHSDALLADA GSGVATLGLP SSPGVTGAAT ADTIVLPYND VDAVDEIFEQ
210 220 230 240 250
VGDQIAAVIT EASPGNMGAV PPEPGFNAAL RRITEEHGAL LILDEVMTGF
260 270 280 290 300
RVSRSGWYGL DPVDGDLFTF GKVMSGGLPA AAFGGRAEVM ERLAPLGPVY
310 320 330 340 350
QAGTLSGNPV AMAAGLATLR TADDAVYAAL DKNADRLAGL LTDALTDAGV
360 370 380 390 400
THRVQRGGNM LSVFFTAEPV GDFATARASE TWRFPPFFHA LLDAGVYPPP
410 420 430
SAFEAWFVSA ALDDEAFDRI AAALPGAARA AAEASRPA
Length:438
Mass (Da):45,467
Last modified:April 3, 2007 - v1
Checksum:iAD889BBC64B9CD10
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000580 Genomic DNA. Translation: ABN96494.1.
RefSeqiWP_011854552.1. NC_009077.1.
YP_001068985.1. NC_009077.1.

Genome annotation databases

EnsemblBacteriaiABN96494; ABN96494; Mjls_0683.
GeneIDi4876427.
KEGGimjl:Mjls_0683.
PATRICi18087489. VBIMycSp51234_0693.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000580 Genomic DNA. Translation: ABN96494.1.
RefSeqiWP_011854552.1. NC_009077.1.
YP_001068985.1. NC_009077.1.

3D structure databases

ProteinModelPortaliA3PUB7.
SMRiA3PUB7. Positions 8-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi164757.Mjls_0683.

Proteomic databases

PRIDEiA3PUB7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN96494; ABN96494; Mjls_0683.
GeneIDi4876427.
KEGGimjl:Mjls_0683.
PATRICi18087489. VBIMycSp51234_0693.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciMSP164757:GHV3-687-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]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JLS.

Entry informationi

Entry nameiGSA_MYCSJ
AccessioniPrimary (citable) accession number: A3PUB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: April 3, 2007
Last modified: January 7, 2015
This is version 66 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

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.