F8A8K0 (F8A8K0_THEID) 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
Ordered Locus Names:	Thein_1218 EMBL AEH45086.1

Organism

Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812) [Complete proteome] [HAMAP] EMBL AEH45086.1

Taxonomic identifier

667014 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Thermodesulfobacteria › Thermodesulfobacteria › Thermodesulfobacteriales › Thermodesulfobacteriaceae › Thermodesulfatator › Thermodesulfatator indicus

Protein attributes

Sequence length	615 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
Domain	Glutamine amidotransferase HAMAP-Rule MF_00164
Molecular function	Aminotransferase HAMAP-Rule MF_00164 EMBL AEH45086.1 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 – 220	219	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	610	1	For Fru-6P isomerization activity By similarity HAMAP-Rule MF_00164

Sequences

	Sequence		Length	Mass (Da)
	F8A8K0 [UniParc]. Last modified September 21, 2011. Version 1. Checksum: 68A8CB98130B2938	FASTA	615	68,585
	10 20 30 40 50 60 MCGIIGYVGP RPVIPVLLEG LRRLEYRGYD SAGVAVLAEG QIDVIRALGK LINLEEILAS 70 80 90 100 110 120 YHKKPEGIGL GHTRWATHGE PAERNAHPHG DCKQELVVVH NGIIENYHHL RASLEAKGHK 130 140 150 160 170 180 FRSQTDTEVI PHLIEEELTK GHSLEEAVRR ALAQVEGSYA IGVFWAKDPK KLIAARNQSP 190 200 210 220 230 240 LVLGLGEGEN FLASDIPALL PWTRKVLFLE DGEMAIITCE ECKIFKLHDA SPVEREPVEI 250 260 270 280 290 300 KWDAAMAEKA GFKHFMLKEI YEQPQAILNT FRGRLDPETG QVKIPEIILS PEEIKSLNKI 310 320 330 340 350 360 CILACGTSYH AGLVGKYLFE RLVRLPVEVE LGSEFRYRDF LIDENTLVIP ISQSGETADT 370 380 390 400 410 420 LASLRRAREA GARAVAICNV LGSTITRESD GTIYTHAGPE IGVASTKAFT SQLTALLLLV 430 440 450 460 470 480 LYFGEIRGTL SEKERKRIAK ALLKVPYQLE KLIEKLHPDI KELSYQYQKK RHFLYLGRNI 490 500 510 520 530 540 LFPIALEGAL KLKEISYIHA EGYAAGEMKH GPIALIDEEM PVVALAPQNH HVYEKMISNI 550 560 570 580 590 600 EEVRSRKGNI FSLGTEGDGT LKRVSQHVLE LPACDWEVSP IIYTVPLQLL AYEVAVRRGC 610 DVDQPRNLAK SVTVE

References

[1]

"The complete genome of Thermodesulfatator indicus DSM 15286." Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders L., Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V. , Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A. Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 15286 / JCM 11887 / CIR29812.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002683 Genomic DNA. Translation: AEH45086.1.
RefSeq	YP_004626050.1. NC_015681.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AEH45086; AEH45086; Thein_1218.
GeneID	10841474.
KEGG	tid:Thein_1218.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K00820.
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

F8A8K0_THEID

Accession

Primary (citable) accession number: F8A8K0

Entry history

Integrated into UniProtKB/TrEMBL:	September 21, 2011
Last sequence update:	September 21, 2011
Last modified:	April 3, 2013
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)