Q12FQ9 (Q12FQ9_POLSJ) 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:	Bpro_0675 EMBL ABE42633.1

Organism

Polaromonas sp. (strain JS666 / ATCC BAA-500) [Complete proteome] [HAMAP] EMBL ABE42633.1

Taxonomic identifier

296591 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Polaromonas

Protein attributes

Sequence length	616 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 ABE42633.1 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 – 227	226	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	611	1	For Fru-6P isomerization activity By similarity HAMAP-Rule MF_00164

Sequences

	Sequence		Length	Mass (Da)
	Q12FQ9 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: F232346143DC1937	FASTA	616	66,422
	10 20 30 40 50 60 MCGIVASVST RNIVPILVQG LQRLEYRGYD SCGVAVYADG LKRARSTSRV AELQSQVDHD 70 80 90 100 110 120 HLQGSTGIAH TRWATHGAPA VHNAHPHFSH GAGANQASRP GKVALVHNGI IENHDELRVA 130 140 150 160 170 180 LQAKGYVFAS QTDTEVIVHL MDSLYDGDLF EALKATVAQL HGAYAIAAFC KDEPHRVVGA 190 200 210 220 230 240 RAGSPLILGV GKGNSENFLA SDAMALAGVT DQIVYLEEGD MVDMQLGKYW VLDRQGKAVQ 250 260 270 280 290 300 RVVKTVQAHS GAAELGPYRH YMQKEIFEQP RAIADTLEGV QGIVPELFGD GAYRVFKEID 310 320 330 340 350 360 SVLILACGTS YYSGCAAKYW LESIAGIPTQ VEVASEYRYR TSVPNPRSLV VTITQSGETA 370 380 390 400 410 420 DTLAALRHAQ SLGMQHTLTI CNVATSAMVR ECKLAYITRA GVEIGVASTK AFTTQLAGLF 430 440 450 460 470 480 LLTLALAQSK GRLTDEAEAE HLKAMRHLPA ALQAVLALEP QVISWSEDFA KMENALFLGR 490 500 510 520 530 540 GLHYPIALEG ALKLKEISYI HAEAYPAGEL KHGPLALVTS AMPVVTVAPN DALLEKLKSN 550 560 570 580 590 600 MQEVRARGGV LYVLADADSH IESGEGLHVI RMPEHYGALS PLLHVVPLQL LAYHTACARG 610 TDVDKPRNLA KSVTVE

References

[1]

"Complete sequence of chromosome of Polaromonas sp. JS666." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Richardson P. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JS666 / ATCC BAA-500.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000316 Genomic DNA. Translation: ABE42633.1.
RefSeq	YP_547531.1. NC_007948.1.
3D structure databases
ProteinModelPortal	Q12FQ9.
SMR	Q12FQ9. Positions 2-616.
ModBase	Search...
Protein-protein interaction databases
STRING	296591.Bpro_0675.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABE42633; ABE42633; Bpro_0675.
GeneID	4011427.
KEGG	pol:Bpro_0675.
PATRIC	22954412. VBIPolSp102244_0693.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0449.
HOGENOM	HOG000258896.
KO	K00820.
OMA	IRLPEHY.
ProtClustDB	PRK00331.
Enzyme and pathway databases
BioCyc	PSP296591:GHI4-1396-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

Q12FQ9_POLSJ

Accession

Primary (citable) accession number: Q12FQ9

Entry history

Integrated into UniProtKB/TrEMBL:	August 22, 2006
Last sequence update:	August 22, 2006
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)