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Protein

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

Gene

GSA

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Cofactori

Pathway:iprotoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (HemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase, chloroplastic (GSA)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Pathway:ichlorophyll biosynthesis

This protein is involved in the pathway chlorophyll biosynthesis, which is part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the pathway chlorophyll biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

GO - Biological processi

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
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030ChloroplastSequence AnalysisAdd
BLAST
Chaini31 – 463433Glutamate-1-semialdehyde 2,1-aminomutase, chloroplasticPRO_0000001257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei303 – 3031N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiQ39566.
ProMEXiQ39566.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi3055.EDP00181.

Structurei

3D structure databases

ProteinModelPortaliQ39566.
SMRiQ39566. Positions 39-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0001.
KOiK01845.
OMAiCGHAHPE.

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]
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.

Q39566-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQMQLNAKTV QGAFKAQRPR SVRGNVAVRA VAAPPKLVTK RSEEIFKEAQ
60 70 80 90 100
ELLPGGVNSP VRAFRSVGGG PIVFDRVKGA YCWDVDGNKY IDYVGSWGPA
110 120 130 140 150
ICGHGNDEVN NALKAQIDKG TSFGAPCELE NVLAKMVIDR VPSVEMVRFV
160 170 180 190 200
SSGTEACLSV LRLMRAYTGR EKVLKFTGCY HGHADSFLVK AGSGVITLGL
210 220 230 240 250
PDSPGVPKST AAATLTATYN NLDSVRELFA ANKGEIAGVI LEPVVGNSGF
260 270 280 290 300
IVPTKEFLQG LREICTAEGA VLCFDEVMTG FRIAKGCAQE HFGITPDLTT
310 320 330 340 350
MGKVIGGGMP VGAYGGKKEI MKMVAPAGPM YQAGTLSGNP MAMTAGIKTL
360 370 380 390 400
EILGRPGAYE HLEKVTKRLI DGIMAAAKEH SHEITGGNIS GMFGFFFCKG
410 420 430 440 450
PVTCFEDALA ADTAKFARFH RGMLEEGVYL APSQFEAGFT SLAHSEADVD
460
ATIAAARRVF ARI
Length:463
Mass (Da):49,228
Last modified:November 1, 1997 - v1
Checksum:i9CB3BDF9A90C8010
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03632 mRNA. Translation: AAA18861.1.
U03633 Unassigned DNA. Translation: AAA18862.1.
PIRiS43787.
RefSeqiXP_001697519.1. XM_001697467.1.
UniGeneiCre.13379.

Genome annotation databases

GeneIDi5723033.
KEGGicre:CHLREDRAFT_138524.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03632 mRNA. Translation: AAA18861.1.
U03633 Unassigned DNA. Translation: AAA18862.1.
PIRiS43787.
RefSeqiXP_001697519.1. XM_001697467.1.
UniGeneiCre.13379.

3D structure databases

ProteinModelPortaliQ39566.
SMRiQ39566. Positions 39-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.EDP00181.

Proteomic databases

PRIDEiQ39566.
ProMEXiQ39566.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5723033.
KEGGicre:CHLREDRAFT_138524.

Phylogenomic databases

eggNOGiCOG0001.
KOiK01845.
OMAiCGHAHPE.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.

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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structure and light-regulated expression of the gsa gene encoding the chlorophyll biosynthetic enzyme, glutamate 1-semialdehyde aminotransferase, in Chlamydomonas reinhardtii."
    Matters G.L., Beale S.I.
    Plant Mol. Biol. 24:617-629(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NO-.

Entry informationi

Entry nameiGSA_CHLRE
AccessioniPrimary (citable) accession number: Q39566
Secondary accession number(s): Q39567
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 22, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.