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Protein

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

Gene

GSA2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Transaminase converting glutamate 1-semialdehyde (GSA) to 5-aminolevulinate (ALA). Involved in the biosynthesis of tetrapyrroles (By similarity).By similarity

Catalytic activityi

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

Cofactori

Pathwayi

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

BioCyciARA:AT3G48730-MONOMER.
UniPathwayiUPA00251; UER00317.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 2, chloroplastic (EC:5.4.3.8)
Short name:
GSA 2
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2
Short name:
GSA-AT 2
Gene namesi
Name:GSA2
Synonyms:HEML2
Ordered Locus Names:At3g48730
ORF Names:T8P19.240
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G48730.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3636ChloroplastBy similarityAdd
BLAST
Chaini37 – 472436Glutamate-1-semialdehyde 2,1-aminomutase 2, chloroplasticPRO_0000001256Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei312 – 3121N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiQ42522.
PRIDEiQ42522.

Expressioni

Gene expression databases

GenevestigatoriQ42522.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi9352. 1 interaction.
MINTiMINT-8069640.
STRINGi3702.AT3G48730.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ42522.
SMRiQ42522. Positions 50-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
InParanoidiQ42522.
KOiK01845.
OMAiCTRENIL.
PhylomeDBiQ42522.

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.

Q42522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATLTGSGI ALGFSCSAKF SKRASSSSNR RCIKMSVSVE EKTKKFTLQK
60 70 80 90 100
SEEAFNAAKN LMPGGVNSPV RAFKSVGGQP VVMDSAKGSR IRDIDGNEYI
110 120 130 140 150
DYVGSWGPAI IGHADDEVLA ALAETMKKGT SFGAPCLLEN VLAEMVISAV
160 170 180 190 200
PSIEMVRFVN SGTEACMGVL RLARAFTGKQ KFIKFEGCYH GHANSFLVKA
210 220 230 240 250
GSGVATLGLP DSPGVPKAAT SDTLTAPYND IAAVEKLFEA NKGEIAAIIL
260 270 280 290 300
EPVVGNSGFI TPKPEFIEGI RRITKDNGAL LIFDEVMTGF RLAYGGAQEY
310 320 330 340 350
FGITPDLTTL GKIIGGGLPV GAYGGRRDIM EMVAPAGPMY QAGTLSGNPL
360 370 380 390 400
AMTAGIHTLK RLSQPGTYEY LDKITKELTN GILEAGKKTG HAMCGGYISG
410 420 430 440 450
MFGFFFTEGP VYDFSDAKKS DTEKFGKFFR GMLEEGVYLA PSQFEAGFTS
460 470
LAHTSEDIQF TIAAAEKVLS RL
Length:472
Mass (Da):50,142
Last modified:June 1, 2001 - v2
Checksum:iE463699500B353FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161C → S in AAA79123 (Ref. 1) Curated
Sequence conflicti194 – 1941N → K in AAA79123 (Ref. 1) Curated
Sequence conflicti283 – 2831F → L in AAA79123 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10278 Genomic DNA. Translation: AAA79123.1.
AL133315 Genomic DNA. Translation: CAB62362.1.
CP002686 Genomic DNA. Translation: AEE78450.1.
BT025324 mRNA. Translation: ABF57280.1.
AK229328 mRNA. Translation: BAF01191.1.
PIRiT46217.
RefSeqiNP_190442.1. NM_114732.4.
UniGeneiAt.19963.

Genome annotation databases

EnsemblPlantsiAT3G48730.1; AT3G48730.1; AT3G48730.
GeneIDi824034.
KEGGiath:AT3G48730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10278 Genomic DNA. Translation: AAA79123.1.
AL133315 Genomic DNA. Translation: CAB62362.1.
CP002686 Genomic DNA. Translation: AEE78450.1.
BT025324 mRNA. Translation: ABF57280.1.
AK229328 mRNA. Translation: BAF01191.1.
PIRiT46217.
RefSeqiNP_190442.1. NM_114732.4.
UniGeneiAt.19963.

3D structure databases

ProteinModelPortaliQ42522.
SMRiQ42522. Positions 50-472.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9352. 1 interaction.
MINTiMINT-8069640.
STRINGi3702.AT3G48730.1-P.

Proteomic databases

PaxDbiQ42522.
PRIDEiQ42522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G48730.1; AT3G48730.1; AT3G48730.
GeneIDi824034.
KEGGiath:AT3G48730.

Organism-specific databases

TAIRiAT3G48730.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
InParanoidiQ42522.
KOiK01845.
OMAiCTRENIL.
PhylomeDBiQ42522.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.
BioCyciARA:AT3G48730-MONOMER.

Miscellaneous databases

PROiQ42522.

Gene expression databases

GenevestigatoriQ42522.

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

« Hide 'large scale' publications
  1. "Nucleotide sequence of a gene encoding glutamate 1-semialdehyde aminotransferase from Arabidopsis thaliana 'Columbia'."
    Wenzlau J.M., Berry-Lowe S.L.
    Plant Gene Register PGR95-007
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Arabidopsis ORF clones."
    Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiGSA2_ARATH
AccessioniPrimary (citable) accession number: Q42522
Secondary accession number(s): Q1JPM9, Q9SMM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 1, 2001
Last modified: April 29, 2015
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.