SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A2BL27

- GSA_HYPBU

UniProt

A2BL27 - GSA_HYPBU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene
hemL, Hbut_0837
Organism
Hyperthermus butylicus (strain DSM 5456 / JCM 9403)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.UniRule annotation

Cofactori

Pyridoxal phosphate By similarity.UniRule 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

BioCyciHBUT415426:GC56-837-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase (EC:5.4.3.8)
Short name:
GSA
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name:
GSA-AT
Gene namesi
Name:hemL
Ordered Locus Names:Hbut_0837
OrganismiHyperthermus butylicus (strain DSM 5456 / JCM 9403)
Taxonomic identifieri415426 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus
ProteomesiUP000002593: Chromosome

Subcellular locationi

Cytoplasm Reviewed prediction 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 – 426426Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotationPRO_1000059991Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Protein-protein interaction databases

STRINGi415426.Hbut_0837.

Structurei

3D structure databases

ProteinModelPortaliA2BL27.
SMRiA2BL27. Positions 3-423.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiHGHANAF.

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.

A2BL27-1 [UniParc]FASTAAdd to Basket

« Hide

MPGEVSRSLY EKALTLFPGG VNSPVRAAVK PYPFYVERAE GPYIYTVDGE    50
KLIDYVLAYG PLILGHKHPR VEEAVRRQLE KGWLYGAPYE LEIRLAEKIL 100
KYYHPGGMVR FVNTGTEATM TAIRLARGVT GRKYIVKFNG CYHGAHDAVL 150
VGAGSAAAEY GVPTSKGIPE EVAKLTLVAK YNDIESVEKI MSKHGDEVAA 200
IIVEPVAGNA GVIPPKKGFL QELRRIASEH GALLIMDEVI TGFRLALGGA 250
QEYYRVKADI TTLGKIVGGG FPIGVVVADR KIMEHLTPSG KVFNAGTFNA 300
HPVTMAAGLA TIEVLEEGTP YRVASEAGRA LAEELESLVL SYGIDAAVNH 350
VESMLQIFFV KGEVWSPEDA AKSDKKLYLK LHEELLKLGV FIAPSQMEAI 400
FTSAAHTSDV VSETIEKLRK AFKRLR 426
Length:426
Mass (Da):46,427
Last modified:February 20, 2007 - v1
Checksum:i7FD5942F85CE8581
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000493 Genomic DNA. Translation: ABM80688.1.
RefSeqiWP_011822006.1. NC_008818.1.
YP_001013033.1. NC_008818.1.

Genome annotation databases

EnsemblBacteriaiABM80688; ABM80688; Hbut_0837.
GeneIDi4782262.
KEGGihbu:Hbut_0837.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000493 Genomic DNA. Translation: ABM80688.1 .
RefSeqi WP_011822006.1. NC_008818.1.
YP_001013033.1. NC_008818.1.

3D structure databases

ProteinModelPortali A2BL27.
SMRi A2BL27. Positions 3-423.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 415426.Hbut_0837.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM80688 ; ABM80688 ; Hbut_0837 .
GeneIDi 4782262.
KEGGi hbu:Hbut_0837.

Phylogenomic databases

eggNOGi COG0001.
HOGENOMi HOG000020210.
KOi K01845.
OMAi HGHANAF.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci HBUT415426:GC56-837-MONOMER.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPi MF_00375. HemL_aminotrans_3.
InterProi IPR004639. 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 ]
PANTHERi PTHR11986. PTHR11986. 1 hit.
Pfami PF00202. Aminotran_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR00713. hemL. 1 hit.
PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
    Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
    Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 5456 / JCM 9403.

Entry informationi

Entry nameiGSA_HYPBU
AccessioniPrimary (citable) accession number: A2BL27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 20, 2007
Last modified: September 3, 2014
This is version 55 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