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Protein

Glutamate-1-semialdehyde 2,1-aminomutase, chloroplastic

Gene

GSA

Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pathwayi

GO - Molecular functioni

  1. glutamate-1-semialdehyde 2,1-aminomutase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro
  3. transaminase activity Source: InterPro

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-UniPathway
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase, chloroplastic (EC:5.4.3.8)
Short name:
GSA
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name:
GSA-AT
Gene namesi
Name:GSA
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Organism-specific databases

GrameneiP18492.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434ChloroplastAdd
BLAST
Chaini35 – 469435Glutamate-1-semialdehyde 2,1-aminomutase, chloroplasticPRO_0000001258Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei309 – 3091N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiP18492.

Expressioni

Gene expression databases

ExpressionAtlasiP18492. baseline.
GenevestigatoriP18492.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP18492.
SMRiP18492. Positions 47-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18492-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGAAAAVAS GISIRPVAAP KISRAPRSRS VVRAAVSIDE KAYTVQKSEE
60 70 80 90 100
IFNAAKELMP GGVNSPVRAF KSVGGQPIVF DSVKGSHMWD VDGNEYIDYV
110 120 130 140 150
GSWGPAIIGH ADDKVNAALI ETLKKGTSFG APCALENVLA QMVISAVPSI
160 170 180 190 200
EMVRFVNSGT EACMGALRLV RAFTGREKIL KFEGCYHGHA DSFLVKAGSG
210 220 230 240 250
VATLGLPDSP GVPKGATVGT LTAPYNDADA VKKLFEDNKG EIAAVFLEPV
260 270 280 290 300
VGNAGFIPPQ PAFLNALREV TKQDGALLVF DEVMTGFRLA YGGAQEYFGI
310 320 330 340 350
TPDVTTLGKI IGGGLPVGAY GGRKDIMEMV APAGPMYQAG TLSGNPLAMT
360 370 380 390 400
AGIHTLKRLM EPGTYEYLDK VTGELVRGIL DVGAKTGHEM CGGHIRGMFG
410 420 430 440 450
FFFAGGPVHN FDDAKKSDTA KFGRFHRGML GEGVYLAPSQ FEAGFTSLAH
460
TTQDIEKTVE AAEKVLRWI
Length:469
Mass (Da):49,494
Last modified:November 1, 1995 - v3
Checksum:i78BF03C14A3C1448
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 3091K → Q AA sequence (PubMed:2505791)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31545 mRNA. Translation: AAB59330.1.
PIRiA35789.
UniGeneiHv.186.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31545 mRNA. Translation: AAB59330.1.
PIRiA35789.
UniGeneiHv.186.

3D structure databases

ProteinModelPortaliP18492.
SMRiP18492. Positions 47-466.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP18492.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GrameneiP18492.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.

Gene expression databases

ExpressionAtlasiP18492. baseline.
GenevestigatoriP18492.

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. "Primary structure of a key enzyme in plant tetrapyrrole synthesis: glutamate 1-semialdehyde aminotransferase."
    Grimm B.
    Proc. Natl. Acad. Sci. U.S.A. 87:4169-4173(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: cv. Bonus.
    Tissue: Seedling.
  2. "Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus."
    Grimm B., Bull A., Welinder K.G., Gough S.P., Kannangara C.G.
    Carlsberg Res. Commun. 54:67-79(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiGSA_HORVU
AccessioniPrimary (citable) accession number: P18492
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.