A8ACN2 (A8ACN2_CITK8) 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:	CKO_00066 EMBL ABV11245.1

Organism

Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) [Complete proteome] [HAMAP] EMBL ABV11245.1

Taxonomic identifier

290338 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter › Citrobacter diversus

Protein attributes

Sequence length	609 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 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 – 218	217	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	604	1	For Fru-6P isomerization activity By similarity HAMAP-Rule MF_00164

Sequences

	Sequence		Length	Mass (Da)
	A8ACN2 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 4EEAD14E4FA70F54	FASTA	609	66,778
	10 20 30 40 50 60 MCGIVGAIAQ RDVAEILLEG LRRLEYRGYD SAGLAVVDAE GHMTRLRRLG KVQMLAQAAE 70 80 90 100 110 120 DHPLSGGTGI AHTRWATHGE PSEANAHPHV SDHIVVVHNG IIENHEPLRE ELKARGYTFV 130 140 150 160 170 180 SETDTEVIAH LVHWELEQGG TLREAVMRAI PQLRGAYGTV IMDTRHPDTL LAARSGSPLV 190 200 210 220 230 240 IGLGMGENFI ASDQLALLPV TRRFIFLEEG DIAEVTRRSV SIFDKSGAEV KRQDIESSLQ 250 260 270 280 290 300 YDAGDKGIYR HYMQKEIYEQ PNAIKNTLTG RISHGEVDLS ELGPKANELL SQVEHIQIIA 310 320 330 340 350 360 CGTSYNSGMV SRYWFESLAG IPCDVEIASE FRYRKSAVRR NSLMITLSQS GETADTLAGL 370 380 390 400 410 420 RLSKELGYLG SLAICNVPGS SLVRESDLAM MTNAGTEIGV ASTKAFTTQL TVLLMLVAKL 430 440 450 460 470 480 ARLKGLDASI EHDIVHGLQA LPSRIEQMLS QDKRIEALAE DFSDKHHALF LGRGDQYPIA 490 500 510 520 530 540 LEGALKLKEI SYIHAEAYAA GELKHGPLAL IDADMPVIVV APNNELLEKL KSNIEEVRAR 550 560 570 580 590 600 GGQLYVFADQ DAGFVSSDNM HIIEMPHVEE VIAPIFYTVP LQLLAYHVAL IKGTDVDQPR NLAKSVTVE

References

[1]

The Citrobacter koseri Genome Sequencing Project McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R. Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-895 / CDC 4225-83 / SGSC4696.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000822 Genomic DNA. Translation: ABV11245.1.
RefSeq	YP_001451681.1. NC_009792.1.
3D structure databases
ProteinModelPortal	A8ACN2.
SMR	A8ACN2. Positions 2-609.
ModBase	Search...
Protein-protein interaction databases
STRING	290338.CKO_00066.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABV11245; ABV11245; CKO_00066.
GeneID	5582308.
KEGG	cko:CKO_00066.
PATRIC	20383616. VBICitKos71230_0060.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0449.
HOGENOM	HOG000258898.
KO	K00820.
OMA	HLVHWEL.
ProtClustDB	PRK00331.
Enzyme and pathway databases
BioCyc	CKOS290338:GJ8L-66-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

A8ACN2_CITK8

Accession

Primary (citable) accession number: A8ACN2

Entry history

Integrated into UniProtKB/TrEMBL:	October 23, 2007
Last sequence update:	October 23, 2007
Last modified:	May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)