A6T3N6 (A6T3N6_JANMA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] HAMAP-Rule MF_00164
EC=2.6.1.16 HAMAP-Rule MF_00164

Alternative name(s):
D-fructose-6-phosphate amidotransferase HAMAP-Rule MF_00164
GFAT HAMAP-Rule MF_00164
Glucosamine-6-phosphate synthase HAMAP-Rule MF_00164
Hexosephosphate aminotransferase HAMAP-Rule MF_00164
L-glutamine--D-fructose-6-phosphate amidotransferase HAMAP-Rule MF_00164

Gene names

Name:	glmS HAMAP-Rule MF_00164 EMBL ABR88336.1
Ordered Locus Names:	mma_3443

Organism

Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis) [Complete proteome] [HAMAP] EMBL ABR88336.1

Taxonomic identifier

375286 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Oxalobacteraceae › Janthinobacterium

Protein attributes

Sequence length	605 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. HAMAP-Rule MF_00164
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00164.
Sequence similarities	Contains 1 glutamine amidotransferase type-2 domain. HAMAP-Rule MF_00164

Ontologies

Keywords
Cellular component	Cytoplasm HAMAP-Rule MF_00164 SAAS SAAS017932
Domain	Glutamine amidotransferase HAMAP-Rule MF_00164
Molecular function	Aminotransferase HAMAP-Rule MF_00164 EMBL ABR88336.1 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 HAMAP-Rule MF_00164
Regions
	Domain	2 – 216	215	Glutamine amidotransferase type-2 By similarity HAMAP-Rule MF_00164
Sites
	Active site	2	1	Nucleophile; for GATase activity By similarity HAMAP-Rule MF_00164
	Active site	600	1	For Fru-6P isomerization activity By similarity HAMAP-Rule MF_00164

Sequences

	Sequence		Length	Mass (Da)
	A6T3N6 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 5104BFCFD2AD0AE8	FASTA	605	66,248
	10 20 30 40 50 60 MCGIVGAVAQ RNITPILVEG LKRLEYRGYD SCGIALHVDG KLERARSTAR VAELEKQIAK 70 80 90 100 110 120 EHLSGFTGIA HTRWATHGAP ASHNAHPHFS RERIALVHNG IIENHDELRD ELKTLGYVFE 130 140 150 160 170 180 SQTDTEVIAH LVDHLYTGDL FETVQTATKR LTGAFAIAVF SRDEPHRVVG ARRGSPLIVG 190 200 210 220 230 240 VGDGENFLAS DALALAGTTD QIIYLEEGDV VDLQLQRVWI VDENGKRVER EVKTVHAHTG 250 260 270 280 290 300 AVELGPYRHY MQKEIFEQPR AISDTLEGIT AITPDIFGDK AYGIFKKIDS VLILACGTSY 310 320 330 340 350 360 YSGMTAKYWI EAVAGVTCNV EIASEYRYRD SVPNPNSLVV TISQSGETAD TLAALRHAQA 370 380 390 400 410 420 QNMRHTLTIC NAATSAMVRE CELAYITRAG VEVGVASTKA FTTQLAALFL LTLSLAQVKG 430 440 450 460 470 480 RLNDEQEAAQ LKAMRHLPSA ITAVLALEPQ IIAWAEAFAR KENALFLGRG LHYPIALEGA 490 500 510 520 530 540 LKLKEISYIH AEAYPAGELK HGPLALVTEE MPVVTVAPND PMIEKLKSNM QEVRARGGEL 550 560 570 580 590 600 YVFADADSRI TSSEGIHVIR LPEHYGLLSP ILHVVPLQLL AYHTALARGT DVDKPRNLAK SVTVE

References

[1]

"Genome analysis of Minibacterium massiliensis highlights the convergent evolution of water-living bacteria." Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D., Drancourt M. PLoS Genet. 3:1454-1463(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Marseille.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000269 Genomic DNA. Translation: ABR88336.1.
RefSeq	YP_001355133.1. NC_009659.1.
3D structure databases
ProteinModelPortal	A6T3N6.
SMR	A6T3N6. Positions 2-605.
ModBase	Search...
Protein-protein interaction databases
STRING	375286.mma_3443.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABR88336; ABR88336; mma_3443.
GeneID	5350408.
KEGG	mms:mma_3443.
PATRIC	22159415. VBIJanSp106498_3464.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0449.
HOGENOM	HOG000258896.
KO	K00820.
OMA	IRLPEHY.
ProtClustDB	PRK00331.
Enzyme and pathway databases
BioCyc	JSP375286:GJ8U-3494-MONOMER.
Family and domain databases
HAMAP	MF_00164. GlmS.
InterPro	IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR005855. GlmS_trans. IPR001347. SIS. [Graphical view]
PANTHER	PTHR10937:SF0. PTHR10937:SF0. 1 hit.
Pfam	PF00310. GATase_2. 1 hit. 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

A6T3N6_JANMA

Accession

Primary (citable) accession number: A6T3N6

Entry history

Integrated into UniProtKB/TrEMBL:	August 21, 2007
Last sequence update:	August 21, 2007
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)