Q3ALU9 (GSA_SYNSC) 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:	Syncc9605_0659

Organism

Synechococcus sp. (strain CC9605) [Complete proteome] [HAMAP]

Taxonomic identifier

110662 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus

Protein attributes

Sequence length	428 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 Porphyrin biosynthesis; chlorophyll biosynthesis. 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	Chlorophyll biosynthesis 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 – 428	428	Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375		PRO_0000243627
Amino acid modifications
	Modified residue	267	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3ALU9 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: 796454BDC0D7964E	FASTA	428	44,785
	10 20 30 40 50 60 MNTSHSQAIF GAAQALMPGG VSSPVRAFKS VGGQPIVFDR VKGPYAWDVD GNKYIDYIGS 70 80 90 100 110 120 WGPAICGHAH PEVIAALQEA IEKGTSFGAP CALENTLAEM VIDAVPSVEM VRFVNSGTEA 130 140 150 160 170 180 CMAVLRLIRA YTGRDKVIKF EGCYHGHADM FLVKAGSGVA TLGLPDSPGV PRSTTANTLT 190 200 210 220 230 240 APYNDLEAVK ALFAENPEAI AGVILEPIVG NAGFIQPEPG FLEGLRELTK EHGALLVFDE 250 260 270 280 290 300 VMTGFRISYG GAQAHFGVTP DLTTMGKVIG GGLPVGAYGG RADIMGMVAP AGPMYQAGTL 310 320 330 340 350 360 SGNPLAMTAG IKTLELLKQP GTYEKLTATT QKLVAGIKDA AQSAGMSITA ASVSAMFGFF 370 380 390 400 410 420 LCEGPVRNFE EAKATDSERF GKLHRAMLEH GVYLAPSAFE AGFTSLAHSE ADIEATINAF RESFAAVA

References

[1]

"Complete sequence of Synechococcus sp. CC9605." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CC9605.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000110 Genomic DNA. Translation: ABB34433.1.
RefSeq	YP_380988.1. NC_007516.1.
3D structure databases
ProteinModelPortal	Q3ALU9.
SMR	Q3ALU9. Positions 3-427.
ModBase	Search...
Protein-protein interaction databases
STRING	110662.Syncc9605_0659.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABB34433; ABB34433; Syncc9605_0659.
GeneID	3736584.
KEGG	syd:Syncc9605_0659.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0001.
HOGENOM	HOG000020210.
KO	K01845.
OMA	FGHADEE.
ProtClustDB	PRK00062.
Enzyme and pathway databases
UniPathway	UPA00251; UER00317. UPA00668.
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_SYNSC

Accession

Primary (citable) accession number: Q3ALU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	November 22, 2005
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program