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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Magnetococcus sp. (strain MC-1)
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

BioCyciMSP156889:GH36-94-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:Mmc1_0093
OrganismiMagnetococcus sp. (strain MC-1)
Taxonomic identifieri156889 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus
ProteomesiUP000002586: 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 – 433433Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000382342Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi156889.Mmc1_0093.

Structurei

3D structure databases

ProteinModelPortaliA0L3S9.
SMRiA0L3S9. Positions 9-429.
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.

A0L3S9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQRGGTMSR SASLFQQAAG LIPGGVNSPV RAFKSVGGIP PFIREAAGAM
60 70 80 90 100
MTDEDGKSYI DYVGSWGPMI LGHAPKEVVA AIQQAAVRGC SFGAPTSNEI
110 120 130 140 150
LLAQKLIELV PSLEMVRLVN SGTEATMSAL RLARAATGRD AILKFDGCYH
160 170 180 190 200
GHADSLLVAA GSGLATFGVP SSPGVTRGTA KDTLTVPFND LAAVEACFAQ
210 220 230 240 250
HPEGIAAVIV EPVAGNMGCV LPRPGYLKGL RDICTKYGTI LIFDEVMTGF
260 270 280 290 300
RVDLRCAQGF YDVTPDLTCL GKVIGGGLPV GAYGGKMELM NQVSPAGPVY
310 320 330 340 350
QAGTLSGNPL ATAAGLATLE AISQPGFYET LTSRTQRLTV GIGKALDEAG
360 370 380 390 400
IPHVSYHIGS MFGLFFTDAR EVYNFADAAK NDHNRFKDWF HCMLEEGVYF
410 420 430
APSPYEAGFV SIAHDEAIID LTIEKARKVA KTL
Length:433
Mass (Da):45,676
Last modified:December 12, 2006 - v1
Checksum:i3537303493DCA1B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000471 Genomic DNA. Translation: ABK42622.1.
RefSeqiYP_864028.1. NC_008576.1.

Genome annotation databases

EnsemblBacteriaiABK42622; ABK42622; Mmc1_0093.
GeneIDi4481094.
KEGGimgm:Mmc1_0093.
PATRICi22426646. VBIMagSp23654_0094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000471 Genomic DNA. Translation: ABK42622.1.
RefSeqiYP_864028.1. NC_008576.1.

3D structure databases

ProteinModelPortaliA0L3S9.
SMRiA0L3S9. Positions 9-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi156889.Mmc1_0093.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK42622; ABK42622; Mmc1_0093.
GeneIDi4481094.
KEGGimgm:Mmc1_0093.
PATRICi22426646. VBIMagSp23654_0094.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciMSP156889:GH36-94-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: MC-1.

Entry informationi

Entry nameiGSA_MAGSM
AccessioniPrimary (citable) accession number: A0L3S9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: December 12, 2006
Last modified: January 7, 2015
This is version 60 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.