Q890U2 (GLMS_CLOTE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
EC=2.6.1.16

Alternative name(s):
D-fructose-6-phosphate amidotransferase
GFAT
Glucosamine-6-phosphate synthase
Hexosephosphate aminotransferase
L-glutamine--D-fructose-6-phosphate amidotransferase

Gene names

Name:	glmS
Ordered Locus Names:	CTC_02543

Organism

Clostridium tetani (strain Massachusetts / E88) [Complete proteome] [HAMAP]

Taxonomic identifier

212717 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium tetani

Protein attributes

Sequence length	608 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source By similarity. HAMAP-Rule MF_00164
Catalytic activity	L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate. HAMAP-Rule MF_00164
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Contains 1 glutamine amidotransferase type-2 domain. Contains 2 SIS domains.
Sequence caution	The sequence AAO37003.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Glutamine amidotransferase Repeat
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	carbohydrate biosynthetic process Inferred from electronic annotation. Source: InterPro glutamine metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro glutamine-fructose-6-phosphate transaminase (isomerizing) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 608	607	Glutamine--fructose-6-phosphate aminotransferase [isomerizing] HAMAP-Rule MF_00164		PRO_0000135324
Regions
	Domain	2 – 217	216	Glutamine amidotransferase type-2
	Domain	284 – 424	141	SIS 1
	Domain	453 – 598	146	SIS 2
Sites
	Active site	2	1	Nucleophile; for GATase activity By similarity
	Active site	603	1	For Fru-6P isomerization activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q890U2 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 01F969978DE4D07E	FASTA	608	67,826
	10 20 30 40 50 60 MCGIVGYIGK KEAAPILVEG LSKLEYRGYD SAGVAIIEDQ VIRTRKCKGR LVNLEEKLNE 70 80 90 100 110 120 ESMIGDIGIG HTRWATHGEP SDKNSHPHNN EKGTISVVHN GIIENYIELR EWLTSEGYKF 130 140 150 160 170 180 VSETDTEVLP HLIDYYYKGD LLEAVMTAIS KVEGSYAIGV VCSEEPDKVV AVRKDSPLIV 190 200 210 220 230 240 GLGEEEYFIA SDIPAVLNHT RDIYLLKDNE FVLMTKDGVK LFDKEGKEIK REIYHVTWNA 250 260 270 280 290 300 DAAEKGGYDH FMLKEIHEQP KVIKDTMTSR IMLGKDIKLD NIEISKEQME KINKIYIVAC 310 320 330 340 350 360 GTAYHAGLVG KYTIEKLARI PVEVDIASEF RYKNPIIDKD TLMIVISQSG ETADTLAALR 370 380 390 400 410 420 EAKKKGARVI AVTNVVGSSI SREADDILYT WAGPEIAVAS TKAYETQLVA MYILALYFAQ 430 440 450 460 470 480 EKGTLNKEEL EELKEEMLSI PDKAEKCLET DEIMKKLASK THMKKDMFFL GRGLDYAVAL 490 500 510 520 530 540 EGSLKLKEIS YIHSEAYAAG ELKHGPIALI EEGTIVITLA TQEELFDKTV SNIKEVTTRG 550 560 570 580 590 600 AKAIGIAFEG QKNMDKAVEE AIYIPKTKSI FAPLLSVIPL QLYSYYVSLE KGCDVDKPRN LAKSVTVE

References

[1]

"The genome sequence of Clostridium tetani, the causative agent of tetanus disease." Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G. Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Massachusetts / E88.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015927 Genomic DNA. Translation: AAO37003.1. Different initiation.
RefSeq	NP_783066.1. NC_004557.1.
3D structure databases
ProteinModelPortal	Q890U2.
ModBase	Search...
Protein-protein interaction databases
STRING	212717.CTC02543.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO37003; AAO37003; CTC_02543.
GeneID	1060148.
KEGG	ctc:CTC02543.
PATRIC	19513205. VBICloTet101274_2633.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0449.
KO	K00820.
OMA	CLQGLER.
ProtClustDB	PRK00331.
Enzyme and pathway databases
BioCyc	CTET212717:GJAM-2350-MONOMER.
Family and domain databases
HAMAP	MF_00164. GlmS.
InterPro	IPR017932. GATase_2_dom. IPR005855. GlmS_trans. IPR001347. SIS. [Graphical view]
PANTHER	PTHR10937:SF0. PTHR10937:SF0. 1 hit.
Pfam	PF01380. SIS. 2 hits. [Graphical view]
TIGRFAMs	TIGR01135. glmS. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. PS51464. SIS. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMS_CLOTE

Accession

Primary (citable) accession number: Q890U2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program