D6Y3G8 (D6Y3G8_THEBD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
Short name=GSA HAMAP-Rule MF_00375
EC=5.4.3.8 HAMAP-Rule MF_00375

Alternative name(s):
Glutamate-1-semialdehyde aminotransferase HAMAP-Rule MF_00375

Gene names

Name:	hemL HAMAP-Rule MF_00375
Ordered Locus Names:	Tbis_0266 EMBL ADG86997.1

Organism

Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / NBRC 14880 / R51) [Complete proteome] [HAMAP] EMBL ADG86997.1

Taxonomic identifier

469371 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Thermobispora › Thermobispora bispora

Protein attributes

Sequence length	432 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 SAAS SAAS004639
Cofactor	Pyridoxal phosphate By similarity. HAMAP-Rule MF_00375 SAAS SAAS004639
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_00375
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00375 SAAS SAAS004639.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily. HAMAP-Rule MF_00375

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis HAMAP-Rule MF_00375 Porphyrin biosynthesis HAMAP-Rule MF_00375 SAAS SAAS004639
Cellular component	Cytoplasm HAMAP-Rule MF_00375 SAAS SAAS004639
Ligand	Pyridoxal phosphate HAMAP-Rule MF_00375 SAAS SAAS004639
Molecular function	Isomerase HAMAP-Rule MF_00375 SAAS SAAS004639
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
Amino acid modifications
	Modified residue	266	1	N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_00375

Sequences

	Sequence		Length	Mass (Da)
	D6Y3G8 [UniParc]. Last modified August 10, 2010. Version 1. Checksum: 20CA78F2DF87CEE2	FASTA	432	45,337
	10 20 30 40 50 60 MTRTQTSEAL FDRAKKIVPG GVNSPVRAFG AVGGTPRFMA SGEGPYLVDV DGNRYVDLVC 70 80 90 100 110 120 SWGPLILGHR HAAVVQAVEE ALSRGLSYGT ATEGEVLLAE EIVSRMPPVE KIRLVSSGTE 130 140 150 160 170 180 ATMSAVRLAR GFTGRSKVIK FAGCYHGHVD ALLASAGSGV ATFGLPDSPG VTGAAAADTI 190 200 210 220 230 240 VLPYNSVEAV EEAFRKFEIA CVITEACPAN MGVVPPAEGF NRRLRELCSE HGALLIIDEV 250 260 270 280 290 300 LTGFRVTAQG WYGVDPVDAD LMTFGKVMGG GLPAAAFGGR ADVMAHLAPE GPVYQAGTLS 310 320 330 340 350 360 GNPLAVAAGL ATLRACDQAV YDRLDRVAET IGRAASEALS AAGVPHRLQR AGNLFSIFFT 370 380 390 400 410 420 DRPVVDYESA RAQDTAAYRA FFHSMLDQGV YLPPSAFEAW FVSAAHDDEA VNRVLEALPA 430 AARAAAQAAR QG

References

[1]

"The complete genome of Thermobispora bispora DSM 43833." US DOE Joint Genome Institute (JGI-PGF) Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F. , Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A. Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / NBRC 14880 / R51.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001874 Genomic DNA. Translation: ADG86997.1.
RefSeq	YP_003650890.1. NC_014165.1.
3D structure databases
ProteinModelPortal	D6Y3G8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ADG86997; ADG86997; Tbis_0266.
GeneID	9166742.
KEGG	tbi:Tbis_0266.
PATRIC	38283424. VBITheBis80272_0269.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000020210.
KO	K01845.
Enzyme and pathway databases
BioCyc	TBIS469371:GHSI-273-MONOMER.
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.
ProtoNet	Search...

Entry information

Entry name

D6Y3G8_THEBD

Accession

Primary (citable) accession number: D6Y3G8

Entry history

Integrated into UniProtKB/TrEMBL:	August 10, 2010
Last sequence update:	August 10, 2010
Last modified:	May 29, 2013
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)