A3MWW7 (GSA_PYRCJ) 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:	Pcal_1717

Organism

Pyrobaculum calidifontis (strain JCM 11548 / VA1) [Complete proteome] [HAMAP]

Taxonomic identifier

410359 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Pyrobaculum › Pyrobaculum calidifontis

Protein attributes

Sequence length	441 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 – 441	441	Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375		PRO_1000059999
Amino acid modifications
	Modified residue	273	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3MWW7 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 4378A5746A3C2705	FASTA	441	47,718
	10 20 30 40 50 60 MPFDVQFLKV FDGVLMLFER AKAVFPGGVN SPARALKHLP TPLVAKAASG PYLYTDRGRL 70 80 90 100 110 120 VDFCLAFGAI ILGHAHPKVR RAVEEQLARG WIYALLTEEE VLFAEKIRAH VPSVEKMRFV 130 140 150 160 170 180 NSGTEATMNA VRLARGFTGR DYIIKFDGNF HGSHDYVLVK AGSGAATWGI PTSAGIPSDV 190 200 210 220 230 240 VKMTVVVPYN DVDAFVKAVR EVGDRLAAVI VEPIAGNYGL ILPEVEFLKA LREETERVGA 250 260 270 280 290 300 LLIFDEVITG FRVGLGGAQG LYGVVPDLTT LGKVIGGGFP IGVFGGKSFI MDLVAPQGPV 310 320 330 340 350 360 YNAGTFNAHP VSIAAGLAVL EELEGGQVYS VANDAARRMA EGIRDLAERV GFDVVVKHIA 370 380 390 400 410 420 SMFQFYFKKG DVKTPQDVRE SNEKLYLKLH ELAIGHGVYL APSQFEVNFT SAAHTAEVVE 430 440 EALGALEKVF RELRREVGGN S

References

[1]

"Complete sequence of Pyrobaculum calidifontis JCM 11548." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCM 11548 / VA1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000561 Genomic DNA. Translation: ABO09134.1.
RefSeq	YP_001056600.1. NC_009073.1.
3D structure databases
ProteinModelPortal	A3MWW7.
SMR	A3MWW7. Positions 15-434.
ModBase	Search...
Protein-protein interaction databases
STRING	410359.Pcal_1717.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABO09134; ABO09134; Pcal_1717.
GeneID	4908200.
KEGG	pcl:Pcal_1717.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0001.
HOGENOM	HOG000020210.
KO	K01845.
OMA	FNGNPIS.
ProtClustDB	PRK00062.
Enzyme and pathway databases
BioCyc	PCAL410359:GIX2-1753-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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSA_PYRCJ

Accession

Primary (citable) accession number: A3MWW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	April 3, 2007
Last modified:	May 29, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program