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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Lactobacillus reuteri (strain DSM 20016)
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

BioCyciLREU557436:GC7Y-1783-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:Lreu_1700
OrganismiLactobacillus reuteri (strain DSM 20016)
Taxonomic identifieri557436 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
ProteomesiUP000001991 Componenti: 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 – 431431Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000382324Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei270 – 2701N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi557436.Lreu_1700.

Structurei

3D structure databases

ProteinModelPortaliA5VM65.
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.

A5VM65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLDTTKSK IAFKEAQKYM PGGVNSPVRA FKNVGGDPLF IDHGKDEYIY
60 70 80 90 100
DIDGNKYIDY VLSWGPLILG HADDHVVAEL DKAVAKGTSY GAPTLQETEL
110 120 130 140 150
AKIVNKIMPS IEMIRMVSSG TEATMSAIRL ARGYTHRKKI VKFVGNYHGH
160 170 180 190 200
SDSLLVDAGS GLATFGINTS PGVPDDLAYD TLTVAYNDVA GVKKLFAEHG
210 220 230 240 250
DEIACAIVEP VAGNMGVIPG TQEFLQTLRN VTNEHGALLI FDEVMSGFRA
260 270 280 290 300
AYHGVQSLVN ITPDLTTLGK VIGGGLPVGA FGGRREIMEN ITPAGDIYHA
310 320 330 340 350
GTLSGNPLAM TGGISTLEQL TPDDYVEMDK KVTALTEGIK HAADQYGVPM
360 370 380 390 400
TVHHVGTMWS YFYNSDPINN FDDVKACDQK LFEKCFWELL AHGVYVAPSQ
410 420 430
FETNFISTKH TDEDIEKTIA AFDAAFNAAT K
Length:431
Mass (Da):46,682
Last modified:July 10, 2007 - v1
Checksum:i8B831E94962EF36C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000705 Genomic DNA. Translation: ABQ83939.1.
RefSeqiWP_011953571.1. NC_009513.1.
YP_001272276.1. NC_009513.1.

Genome annotation databases

EnsemblBacteriaiABQ83939; ABQ83939; Lreu_1700.
KEGGilre:Lreu_1700.
PATRICi22256661. VBILacReu87937_1718.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000705 Genomic DNA. Translation: ABQ83939.1.
RefSeqiWP_011953571.1. NC_009513.1.
YP_001272276.1. NC_009513.1.

3D structure databases

ProteinModelPortaliA5VM65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi557436.Lreu_1700.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ83939; ABQ83939; Lreu_1700.
KEGGilre:Lreu_1700.
PATRICi22256661. VBILacReu87937_1718.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciLREU557436:GC7Y-1783-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 20016.

Entry informationi

Entry nameiGSA_LACRD
AccessioniPrimary (citable) accession number: A5VM65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: July 10, 2007
Last modified: April 1, 2015
This is version 69 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.