A2BVE5 (GSA_PROM5) 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:	P9515_05471

Organism

Prochlorococcus marinus (strain MIT 9515) [Complete proteome] [HAMAP]

Taxonomic identifier

167542 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Prochlorales › Prochlorococcaceae › Prochlorococcus › Prochlorococcus marinus

Protein attributes

Sequence length	433 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.
Sequence caution	The sequence ABM71756.1 differs from that shown. Reason: Erroneous initiation.

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 – 433	433	Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375		PRO_0000382359
Amino acid modifications
	Modified residue	271	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2BVE5 [UniParc]. Last modified September 1, 2009. Version 2. Checksum: 5497134BEBF85809	FASTA	433	46,243
	10 20 30 40 50 60 MTDIFNITHS EEVFSSALKL MPGGVSSPVR AFKSVGGQPI VFDRVKGPFA WDVDGNRYID 70 80 90 100 110 120 YIGSWGPAIC GHAHPEVITA LQEAIEKGTS FGAPCVQENK LAEMVIDAVP SVEMVRFVNS 130 140 150 160 170 180 GTEACMAVLR LMRAFTGRDK VIKFDGCYHG HADMFLVKAG SGVATLGLPD SPGVPRTTTA 190 200 210 220 230 240 NTLTAPYNDL EAVKKLFSEN PDAISGVILE PIVGNAGFIT PEPGFLEGLR ELTTENGSLL 250 260 270 280 290 300 VFDEVMTGFR ISYGGAQEKF GVTPDLTTLG KVIGGGLPVG AYGGRKEIMS MVAPSGPVYQ 310 320 330 340 350 360 AGTLSGNPLA MTAGIKTLEL LKQEGTYEKM GLATSRLIEG IMQSAENNGI AINGGSVSAM 370 380 390 400 410 420 FGFFLCEGPV RNFEEAKTNN SELFGKLHRE MIKRGVYLAP SPFEAGFTSL AHSEEEIDRT 430 IEAFDQSFSV IKN

References

[1]

"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus." Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W. PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MIT 9515.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000552 Genomic DNA. Translation: ABM71756.1. Different initiation.
RefSeq	YP_001010863.1. NC_008817.1.
3D structure databases
ProteinModelPortal	A2BVE5.
ModBase	Search...
Protein-protein interaction databases
STRING	167542.P9515_05471.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABM71756; ABM71756; P9515_05471.
GeneID	4719765.
KEGG	pmc:P9515_05471.
PATRIC	23014674. VBIProMar113831_0566.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0001.
HOGENOM	HOG000020210.
KO	K01845.
ProtClustDB	PRK00062.
Enzyme and pathway databases
BioCyc	PMAR167542:GI3N-529-MONOMER.
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_PROM5

Accession

Primary (citable) accession number: A2BVE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 1, 2009
Last sequence update:	September 1, 2009
Last modified:	May 1, 2013
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program