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

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P42799 (GSA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 1, chloroplastic
Short name=GSA 1
EC=5.4.3.8

Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1
Short name=GSA-AT 1

Gene names

Name:	GSA1
Ordered Locus Names:	At5g63570
ORF Names:	MBK5.3

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.
Cofactor	Pyridoxal phosphate.
Pathway	Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
Subunit structure	Homodimer By similarity.
Subcellular location	Plastid › chloroplast.
Tissue specificity	Present in all tissues tested.
Induction	By light. In etiolated seedlings, initial expression is reduced but after further illumination, levels steadily increase.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis Porphyrin biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	apoplast Inferred from direct assay PubMed 18538804. Source: TAIR chloroplast envelope Inferred from direct assay PubMed 12938931. Source: TAIR chloroplast stroma Inferred from direct assay PubMed 16207701 PubMed 18633119 PubMed 20061580. Source: TAIR
Molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transaminase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRL1	Q9ZPS9	1	EBI-2293485,EBI-2292728

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 38

Chloroplast By similarity

Chain

39 – 474

436

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

PRO_0000001255

Amino acid modifications

Modified residue

314

N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P42799 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 0D5E1A84F2B7433E
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FASTA

474

50,370

        10         20         30         40         50         60 
MSATLTGSGT ALGFSCSSKI SKRVSSSPAS NRCCIKMSVS VDEKKKSFSL QKSEEAFNAA 

        70         80         90        100        110        120 
KNLMPGGVNS PVRAFKSVGG QPVLIDSVKG SKMWDIDGNE YIDYVGSWGP AIIGHADDEV 

       130        140        150        160        170        180 
LAALAETMKK GTSFGAPCLL ENVLAEMVIS AVPSIEMVRF VNSGTEACMG VLRLARAFTN 

       190        200        210        220        230        240 
KEKFIKFEGC YHGHANAFLV KAGSGVATLG LPDSPGVPKA ATSDTLTAPY NDLEAVEKLF 

       250        260        270        280        290        300 
AAHKGEISAV ILEPVVGNSG FIPPTPEFIN GLRQLTKDNG VLLIFDEVMT GFRLAYGGAQ 

       310        320        330        340        350        360 
EYFGITPDLT TLGKIIGGGL PVGAYGGRRD IMEMVAPAGP MYQAGTLSGN PLAMTAGIHT 

       370        380        390        400        410        420 
LKRLKQAGTY EYLDKITKEL TNGILEAGKK TGHPMCGGYI SGMFGFFFAE GPVYNFADSK 

       430        440        450        460        470 
KSDTEKFGRF FRGMLEEGVY FAPSQFEAGF TSLAHTPEDI QLTIAAAERV LSRI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis." Ilag L.L., Kumar A.M., Soell D. Plant Cell 6:265-275(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia. Tissue: Leaf.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones." Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S. DNA Res. 4:215-230(1997) [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]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U03773 Genomic DNA. Translation: AAA19117.1. AB005234 Genomic DNA. Translation: BAB10450.1. CP002688 Genomic DNA. Translation: AED97770.1. AY102109 mRNA. Translation: AAM26679.1. AY139804 mRNA. Translation: AAM98110.1.
IPI	IPI00529380.
RefSeq	NP_201162.1. NM_125752.3.
UniGene	At.27758.
3D structure databases
ProteinModelPortal	P42799.
SMR	P42799. Positions 52-474.
ModBase	Search...
Protein-protein interaction databases
IntAct	P42799. 1 interaction.
STRING	3702.AT5G63570.1-P.
Proteomic databases
PaxDb	P42799.
PRIDE	P42799.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G63570.1; AT5G63570.1; AT5G63570.
GeneID	836476.
KEGG	ath:AT5G63570.
Organism-specific databases
TAIR	At5g63570.
Phylogenomic databases
eggNOG	COG0001.
HOGENOM	HOG000020210.
InParanoid	P42799.
KO	K01845.
OMA	FGHADEE.
PhylomeDB	P42799.
ProtClustDB	PLN02482.
Enzyme and pathway databases
BioCyc	ARA:AT5G63570-MONOMER. MetaCyc:AT5G63570-MONOMER.
UniPathway	UPA00251; UER00317. UPA00668.
Gene expression databases
ArrayExpress	P42799.
Genevestigator	P42799.
GermOnline	AT5G63570. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
InterPro	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]
PANTHER	PTHR11986. PTHR11986. 1 hit. PTHR11986:SF5. PTHR11986:SF5. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00713. hemL. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSA1_ARATH

Accession

Primary (citable) accession number: P42799

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents