Q2JMP7 (GSA_SYNJB) 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:	CYB_1012

Organism

Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) [Complete proteome] [HAMAP]

Taxonomic identifier

321332 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	436 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 – 436	436	Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375		PRO_0000243629
Amino acid modifications
	Modified residue	276	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2JMP7 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: C86B8D6FE5F30730	FASTA	436	46,729
	10 20 30 40 50 60 MTSTLHSTSF NTTRSKQVFA RAQSLMPGGV SSPVRAFKSV GGDPVVFDRV SGAYAWDVDG 70 80 90 100 110 120 NQYIDYIGSW GPAIVGHAHP EVIEALRRAL EKGTSFGAPC VLENELAERV IEAVPSVEMV 130 140 150 160 170 180 RFVNSGTEAC MAVLRLMRAY TGREKVIKFE GCYHGHADMF LVKAGSGVAT LGLPDSPGVP 190 200 210 220 230 240 KAATSATLTA PYNDLEAVKA LFEQHPDSIA GVILEPVVGN AGFIPPQPGF LEGLRDLTQK 250 260 270 280 290 300 YGALLVFDEV MTGFRISYGG VQAKFGVIPD LTTLGKVIGG GLPVGAYGGR REIMEMVAPA 310 320 330 340 350 360 GPMYQAGTLS GNPLAMTAGI QTLDILRRPG TYEYLERITE KLATGLLQIA RETGHEMCGG 370 380 390 400 410 420 YLPGMFGFFF TAGPVRNYEE AKTSDLQKFA RFHRGMLERG VYLAPSQFEA GFTSLAHTEA 430 DVEKTLAAAR EVLSTL

References

[1]

"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses." Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F. ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JA-2-3B'a(2-13).

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000240 Genomic DNA. Translation: ABD01990.1.
RefSeq	YP_477253.1. NC_007776.1.
3D structure databases
ProteinModelPortal	Q2JMP7.
SMR	Q2JMP7. Positions 10-436.
ModBase	Search...
Protein-protein interaction databases
STRING	321332.CYB_1012.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD01990; ABD01990; CYB_1012.
GeneID	3900384.
KEGG	cyb:CYB_1012.
PATRIC	23804332. VBISynSp29577_1023.
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_SYNJB

Accession

Primary (citable) accession number: Q2JMP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program