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Q980U5

- GSA_SULSO

UniProt

Q980U5 - GSA_SULSO

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Protein
Glutamate-1-semialdehyde 2,1-aminomutase
Gene
hemL, SSO0182
Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.1 Publication

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-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:SSO0182
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: 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 – 418418Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation
PRO_0000120490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei260 – 2601N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi273057.SSO0182.

Structurei

3D structure databases

ProteinModelPortaliQ980U5.
SMRiQ980U5. Positions 2-417.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiHYPSIDM.

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

MNSEELWAQA KQLFAGGVNS PVRAAVKPFP FYVERGKGAY IYTVDGKKFI    50
DYVLGYGPLI LGHSPESVKR RIVEQLERGW LFGTPSELEI ELARKIRSHI 100
PSAQKIRFVN SGTEATMAAI RLARGYTKRS KILKFSGNYH GAHDYALVEA 150
GSAATEYNVA TSDGVPMEIM KTVEICEFND LDCVDKKLRN EDIATVILEP 200
VMGNAGVILP EKDFLFGLRE LTKTYNSLLI FDEVITGFRI SIGGAQSYYQ 250
IYPDITTLGK IIGGGFPIGA VAGKAEIIDN FTPAGKVFNA GTFNANPISM 300
IAGIATIEEL EKEYPYIIAN QAAKTLVEEL ERLLKTKHTI NHVGSMFQIF 350
FGIDEVRNYS DAKRADKEYY IKFHERLLKE GVFIPPSQYE TIFTSAAHKD 400
DVIADTIDKL MKVIGELN 418
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251A → F AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE006641 Genomic DNA. Translation: AAK40528.1 . Different initiation.
PIRi A90159.
RefSeqi NP_341738.1. NC_002754.1.

3D structure databases

ProteinModelPortali Q980U5.
SMRi Q980U5. Positions 2-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273057.SSO0182.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK40528 ; AAK40528 ; SSO0182 .
GeneIDi 1455338.
KEGGi sso:SSO0182.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci SSOL273057:GCH2-171-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

« 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: May 14, 2014
This is version 77 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

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