A1WBR8 (GSA_ACISJ) 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:	Ajs_3581

Organism

Acidovorax sp. (strain JS42) [Complete proteome] [HAMAP]

Taxonomic identifier

232721 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length	434 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 – 434	434	Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375		PRO_0000300888
Amino acid modifications
	Modified residue	274	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1WBR8 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 3F61AAF22F22EB9C	FASTA	434	45,915
	10 20 30 40 50 60 MTHNTDLNLP LFERAKALIP GGVNSPVRAF RAVGGTPRFI TRAQGAYMWD ANGQRFIDYI 70 80 90 100 110 120 GSWGPMILGH GHPAVLEAVQ KAALEGFSFG APTEREVELA EEIIRHVPSM EMIRLVSSGT 130 140 150 160 170 180 EAGMSAIRLA RGATRRNKII KFNGCYHGHA DSLLVKAGSG LATFGHATSA GVPQEVVQHT 190 200 210 220 230 240 LVLEYNDVAQ LEEAFTLHGP DVACVIMEPI AGNMNFVRAS VPFMRRAREL CTQHGALLVI 250 260 270 280 290 300 DEVMTGFRVA LGGAQSLYAQ AIPGFKPDIT VLGKVIGGGM PLAAFGGSRA VMEQLAPLGP 310 320 330 340 350 360 VYQAGTLSGN PVATACGLAT LREIAKPGFY DALGARTRAL IDGLAGAASA AGVPLCGDTQ 370 380 390 400 410 420 GGMFGFFLLP QLPQNYPEVL NTDGMRFNTL FHGLLDGGVY IAPALYEAGF VSAAHTEQDI 430 ADTVAVARDV FQKL

References

[1]

"Complete sequence of chromosome 1 of Acidovorax sp. JS42." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JS42.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000539 Genomic DNA. Translation: ABM43693.1.
RefSeq	YP_987769.1. NC_008782.1.
3D structure databases
ProteinModelPortal	A1WBR8.
ModBase	Search...
Protein-protein interaction databases
STRING	232721.Ajs_3581.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABM43693; ABM43693; Ajs_3581.
GeneID	4670580.
KEGG	ajs:Ajs_3581.
PATRIC	20692549. VBIAciSp27161_3791.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0001.
HOGENOM	HOG000020210.
KO	K01845.
OMA	NANIPFF.
ProtClustDB	PRK00062.
Enzyme and pathway databases
BioCyc	ASP232721:GHWE-3644-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_ACISJ

Accession

Primary (citable) accession number: A1WBR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program