A9BY74 (GSA_DELAS) 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:	Daci_1569

Organism

Delftia acidovorans (strain DSM 14801 / SPH-1) [Complete proteome] [HAMAP]

Taxonomic identifier

398578 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Delftia › Delftia acidovorans

Protein attributes

Sequence length	438 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 – 438	438	Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375		PRO_0000382304
Amino acid modifications
	Modified residue	278	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9BY74 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: A4FBE794778D0CBE	FASTA	438	46,977
	10 20 30 40 50 60 MADSCTMTTD LNIPLFERAK AVIPGGVNSP VRAFNAVGGT PRFVRRAQGA HFWDENAQQF 70 80 90 100 110 120 TDYIGSWGPM ILGHGHPEVM AAVQAAALEG FSFGAPTERE VVLAEKILSL MPSMDMVRMV 130 140 150 160 170 180 SSGTEAGMSA LRLARGFTGR NKIIKFNGCY HGHADALLVK AGSGLATFGA SSSAGVPQDV 190 200 210 220 230 240 VKDTVVLEYN DVGQLEEAFA QFGDQIACVI MEPIAGNMNF VRASVPFTRR IRELTREHGA 250 260 270 280 290 300 LMVYDEVMTG FRVALGSAQS LYAQHIEGFA PDITVLGKVI GGGMPMAAFG ARREIMEKLS 310 320 330 340 350 360 PLGPVYQAGT LSGNPIATAC GLKTLELISE PGFHDALHAK TGRLMAGFKA EADAAGVPFS 370 380 390 400 410 420 VDHQGGLFGF YLLPELPSTW TEVMKTDGAR FNRFFHGMLE RGHYFAPALY EAGFVSAAHT 430 DADIDKTIEA AREVFKTL

References

[1]

"Complete sequence of Delftia acidovorans DSM 14801 / SPH-1." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 14801 / SPH-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000884 Genomic DNA. Translation: ABX34213.1.
RefSeq	YP_001562598.1. NC_010002.1.
3D structure databases
ProteinModelPortal	A9BY74.
ModBase	Search...
Protein-protein interaction databases
STRING	398578.Daci_1569.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABX34213; ABX34213; Daci_1569.
GeneID	5747126.
KEGG	dac:Daci_1569.
PATRIC	21637049. VBIDelAci41351_1610.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0001.
HOGENOM	HOG000020210.
KO	K01845.
OMA	ANMIVER.
ProtClustDB	PRK00062.
Enzyme and pathway databases
BioCyc	DACI398578:GHK3-1667-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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSA_DELAS

Accession

Primary (citable) accession number: A9BY74

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 1, 2009
Last sequence update:	January 15, 2008
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program