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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 2

Gene

hemL2

Organism
Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15)
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

BioCyciESIB262543:GHBP-2213-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 2UniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSA 2UniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2UniRule annotation
Short name:
GSA-AT 2UniRule annotation
Gene namesi
Name:hemL2UniRule annotation
Ordered Locus Names:Exig_2134
OrganismiExiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15)
Taxonomic identifieri262543 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium
ProteomesiUP000001681: 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 – 436436Glutamate-1-semialdehyde 2,1-aminomutase 2PRO_0000382314Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei271 – 2711N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiB1YJU8.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi262543.Exig_2134.

Structurei

3D structure databases

ProteinModelPortaliB1YJU8.
SMRiB1YJU8. Positions 39-430.
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.

B1YJU8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLTNQNSKS KAAFERALPL MPGGVNSPVR AYKSVGMTPI FAERAQGSRL
60 70 80 90 100
YDIDGKEYID YVLSWGPMIL GHADPIVTAA IQEQATRGWS YGTPTEIESA
110 120 130 140 150
MAEVVISRVP SVEVVRMVNS GTEATMAALR LARGYTGKTK ILKFEGCYHG
160 170 180 190 200
HGDSLLIKAG SGVATLGLPD SPGVPAQIAS MTLTVPYNDM DAVRIAFEKH
210 220 230 240 250
GDDIAGVIVE PAAGNMGFVP PQPGFLEGLR EITEQHGTLL IFDEVMTGFR
260 270 280 290 300
VGFNCAQGHF GVTPDITCLG KVIGGGMPVG AYGGRRDIME QIAPQGPIYQ
310 320 330 340 350
AGTLSGNPLA MAAGLATLTQ LKPEHYEEFD RKANRLSEGY LAAAAKYNIP
360 370 380 390 400
LTTNRAGAMF GVFFTDQPVT NFEQAKSSNL DMFRSYYQKM AARGVFLPPS
410 420 430
QFEGLFLSTV HTDDDIEQTL AAVELTFKEL QLEFNR
Length:436
Mass (Da):47,038
Last modified:May 20, 2008 - v1
Checksum:i4EB5B02EF18C056D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001022 Genomic DNA. Translation: ACB61586.1.
RefSeqiYP_001814603.1. NC_010556.1.

Genome annotation databases

EnsemblBacteriaiACB61586; ACB61586; Exig_2134.
GeneIDi6173802.
KEGGiesi:Exig_2134.
PATRICi32137892. VBIExiSib53410_2169.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001022 Genomic DNA. Translation: ACB61586.1.
RefSeqiYP_001814603.1. NC_010556.1.

3D structure databases

ProteinModelPortaliB1YJU8.
SMRiB1YJU8. Positions 39-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262543.Exig_2134.

Proteomic databases

PRIDEiB1YJU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB61586; ACB61586; Exig_2134.
GeneIDi6173802.
KEGGiesi:Exig_2134.
PATRICi32137892. VBIExiSib53410_2169.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciESIB262543:GHBP-2213-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: DSM 17290 / JCM 13490 / 255-15.

Entry informationi

Entry nameiGSA2_EXIS2
AccessioniPrimary (citable) accession number: B1YJU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 20, 2008
Last modified: January 7, 2015
This is version 54 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.