Q976H2 (GSA_SULTO) 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:	STK_02150

Organism

Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) [Complete proteome] [HAMAP]

Taxonomic identifier

273063 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus › Sulfolobus tokodaii

Protein attributes

Sequence length	419 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. HAMAP-Rule MF_00375
Pathway	Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
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 – 419	419	Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375		PRO_0000120491
Amino acid modifications
	Modified residue	259	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q976H2 [UniParc]. Last modified December 14, 2011. Version 3. Checksum: E547DE1E895C56AB	FASTA	419	46,198
	10 20 30 40 50 60 MSENLWKKAL ELFAGGVNSP VRAAVKPYPF YVEKSEGAFL YTIDGQRLID YVLGYGPLIL 70 80 90 100 110 120 GHAHPYVKKK IIEQIEKGWL YGTPSKKEIE LAEKIRSHIP SAEKIRFVNS GTEATMLAIR 130 140 150 160 170 180 LARGYTKREK ILKFDGNYHG AHDYALINAG SAVSEFNVII SSGIPTSIIN TVIVCKYNDL 190 200 210 220 230 240 DCVEKHLRTE EIAGVIVEPV MGNMGVILPE QDFLNGLREL TKTYNSVLIF DEVITGFRLG 250 260 270 280 290 300 LSGAQGYFKV IPDLTTLGKI IGGGLPIGAV TGKKEIMSNL TPEGKVFNAG TFNANPLTMA 310 320 330 340 350 360 AGIATIEVLE TTNAYDIANK ASKEIAEELD NSLSKKNFKY TINRIQSMFQ FFIGISKVTN 370 380 390 400 410 ADDARLANKD LYVKIHEKLL KLGVFIPPSQ FETIFTSSSH SDEIVNLTIE AIHKVVSEI

References

[1]

"Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7." Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H. DNA Res. 8:123-140(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000023 Genomic DNA. Translation: BAK54198.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	273063.ST0215.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAK54198; BAK54198; STK_02150.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0001.
HOGENOM	HOG000020210.
Enzyme and pathway databases
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSA_SULTO

Accession

Primary (citable) accession number: Q976H2
Secondary accession number(s): F9VMQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	December 14, 2011
Last modified:	May 29, 2013
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program