Q5WWG1 (GSA_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	hemL
Ordered Locus Names:	lpl1492

Organism

Legionella pneumophila (strain Lens) [Complete proteome] [HAMAP]

Taxonomic identifier

297245 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella › Legionella pneumophila

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00375.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: HAMAP protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transaminase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 429	429	Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375		PRO_0000243580
Amino acid modifications
	Modified residue	265	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5WWG1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 348F41F00F500E64	FASTA	429	46,168
	10 20 30 40 50 60 MSRSSDLFHK AQTIIPGGVN SPVRAFKGVG GEPVFFKSGK GAYLTDVDDK QYIDYVGSWG 70 80 90 100 110 120 PLILGHCHPK VIEAVDNVLH SGMSFGAPTE LEIQLAEKIA SLMPSIEKIR MVNSGTEATM 130 140 150 160 170 180 TAIRLARGFT NKNKFIKFNG CYHGHSDSLL VKAGSGLLTL GIPSTPGIPQ CITEHTLTAD 190 200 210 220 230 240 FNNLEQVAQL FEKYPNDIAT VILEPVPGNM GFILPKIEFL KGLRELCDQY NALLIFDEVM 250 260 270 280 290 300 TGFRVGLHGA QGLFGIKPDI TTLGKIIGGG MPVGALGGKR EIMSFLAPEG PVYQAGTLSG 310 320 330 340 350 360 NPLAMAAGLA TLKEIEKINF FEDLSSTTNK LTEALSDAAE NANIPLFAAS LGGMFGFCFT 370 380 390 400 410 420 DKNSVENYLD VASSDEVLFK KFFHAMLAQG VYFAPSMYEA GFVSSMHGDL EIQKTYDAAE LVLNQLKSA

References

[1]

"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity." Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C. Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Lens.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR628337 Genomic DNA. Translation: CAH15732.1.
RefSeq	YP_126838.1. NC_006369.1.
3D structure databases
ProteinModelPortal	Q5WWG1.
SMR	Q5WWG1. Positions 33-426.
ModBase	Search...
Protein-protein interaction databases
STRING	297245.lpl1492.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAH15732; CAH15732; lpl1492.
GeneID	3115208.
KEGG	lpf:lpl1492.
PATRIC	22316671. VBILegPne33733_1662.
Organism-specific databases
LegioList	lpl1492.
CMR	Search...
Phylogenomic databases
eggNOG	COG0001.
HOGENOM	HOG000020210.
KO	K01845.
OMA	FNGNPIS.
ProtClustDB	PRK00062.
Enzyme and pathway databases
BioCyc	LPNE297245:GJD4-1610-MONOMER.
UniPathway	UPA00251; UER00317.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
HAMAP	MF_00375. HemL_aminotrans_3.
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

GSA_LEGPL

Accession

Primary (citable) accession number: Q5WWG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	November 23, 2004
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program