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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.1 PublicationUniRule annotation

Cofactori

pyridoxal 5'-phosphate1 PublicationUniRule annotation

Enzyme regulationi

Inhibited by gabaculine.1 Publication

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

BioCyciSSOL273057:GCH2-171-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:SSO0182
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: 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 – 418418Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei260 – 2601N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.1 PublicationUniRule annotation

Protein-protein interaction databases

STRINGi273057.SSO0182.

Structurei

3D structure databases

ProteinModelPortaliQ980U5.
SMRiQ980U5. Positions 2-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
InParanoidiQ980U5.
KOiK01845.
OMAiACLMIEP.

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.

Q980U5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNSEELWAQA KQLFAGGVNS PVRAAVKPFP FYVERGKGAY IYTVDGKKFI
60 70 80 90 100
DYVLGYGPLI LGHSPESVKR RIVEQLERGW LFGTPSELEI ELARKIRSHI
110 120 130 140 150
PSAQKIRFVN SGTEATMAAI RLARGYTKRS KILKFSGNYH GAHDYALVEA
160 170 180 190 200
GSAATEYNVA TSDGVPMEIM KTVEICEFND LDCVDKKLRN EDIATVILEP
210 220 230 240 250
VMGNAGVILP EKDFLFGLRE LTKTYNSLLI FDEVITGFRI SIGGAQSYYQ
260 270 280 290 300
IYPDITTLGK IIGGGFPIGA VAGKAEIIDN FTPAGKVFNA GTFNANPISM
310 320 330 340 350
IAGIATIEEL EKEYPYIIAN QAAKTLVEEL ERLLKTKHTI NHVGSMFQIF
360 370 380 390 400
FGIDEVRNYS DAKRADKEYY IKFHERLLKE GVFIPPSQYE TIFTSAAHKD
410
DVIADTIDKL MKVIGELN
Length:418
Mass (Da):46,477
Last modified:September 19, 2006 - v2
Checksum:iC290C1884A38E710
GO

Sequence cautioni

The sequence AAK40528.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251A → F AA sequence (PubMed:8973563)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK40528.1. Different initiation.
PIRiA90159.
RefSeqiNP_341738.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK40528; AAK40528; SSO0182.
GeneIDi1455338.
KEGGisso:SSO0182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK40528.1. Different initiation.
PIRiA90159.
RefSeqiNP_341738.1. NC_002754.1.

3D structure databases

ProteinModelPortaliQ980U5.
SMRiQ980U5. Positions 2-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO0182.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK40528; AAK40528; SSO0182.
GeneIDi1455338.
KEGGisso:SSO0182.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
InParanoidiQ980U5.
KOiK01845.
OMAiACLMIEP.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciSSOL273057:GCH2-171-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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. "Glutamate-1-semialdehyde aminotransferase from Sulfolobus solfataricus."
    Palmieri G., Di Palo M., Scaloni A., Orru S., Marino G., Sannia G.
    Biochem. J. 320:541-545(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-25, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT.
    Strain: DSM 5833 / MT-4.

Entry informationi

Entry nameiGSA_SULSO
AccessioniPrimary (citable) accession number: Q980U5
Secondary accession number(s): Q9UWG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: September 19, 2006
Last modified: January 7, 2015
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.