G0J7R9 (G0J7R9_CYCMS) 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:	Cycma_4059 EMBL AEL27767.1

Organism

Cyclobacterium marinum (strain ATCC 25205 / DSM 745) (Flectobacillus marinus) [Complete proteome] [HAMAP]

Taxonomic identifier

880070 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Bacteroidetes/Chlorobi group › Bacteroidetes › Cytophagia › Cytophagales › Cyclobacteriaceae › Cyclobacterium › Cyclobacterium marinum

Protein attributes

Sequence length	611 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 AEL27767.1 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 – 219	218	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	606	1	For Fru-6P isomerization activity By similarity HAMAP-Rule MF_00164

Sequences

	Sequence		Length	Mass (Da)
	G0J7R9 [UniParc]. Last modified October 19, 2011. Version 1. Checksum: 7DC08114F26B11F1	FASTA	611	67,266
	10 20 30 40 50 60 MCGIVAYIGS REAYPIILKG LQRLEYRGYD SAGVALLDKE LAVYKKMGKV AELESSLIGT 70 80 90 100 110 120 NLHAQSGIGH TRWATHGEPS DRNAHPHRST SGKLAMVHNG IIENFAPIKK ELQQKGYVFE 130 140 150 160 170 180 SDTDTEVLLH FIDDIYQNDA NNLEEAVRIA LKRIVGAYVI ILLDQDQPDT LIAARKGSPL 190 200 210 220 230 240 VIGIGKNEHF LASDASPIIE YTKEVVYIND YEMAIVKPDE LILKNPGNER ITPFITKLDM 250 260 270 280 290 300 ELAAIEKGGY EHFMLKEIFE QPTAVFDCLR GRLDAKKGTI TMGGIDQHLD LLREANRIII 310 320 330 340 350 360 VGCGTSWHAG LLAEYVLEEL CRVPVEVEYA SEFRYRNPVI NPGDVIIAVS QSGETADTLV 370 380 390 400 410 420 ALENAKNKGA FIFGVVNVVG SSIARLSQAG AYTHAGPEIG VASTKAFTAQ LTVLYMIAIK 430 440 450 460 470 480 LGYSKGTLSK ERYQHLINEL SLVPDKIQDA LNEATSIEKL AKKYQHARDF LFLGRGYNFP 490 500 510 520 530 540 IALEGALKLK EISYIHAEGY PAAEMKHGPI ALVEETLPVV FVATRDVYHE KLVSNAREIK 550 560 570 580 590 600 ARKGQVLAVI TENDDLFEEI ADDTISVPAA DELIAPLISV VPLQLLAYYT GLAKGLDVDK 610 PRNLAKSVTV E

References

[1]

"The complete genome of Cyclobacterium marinum DSM 745." Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V. , Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A., Brambilla E., Klenk H.-P., Eisen J.A. Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25205 / DSM 745.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002955 Genomic DNA. Translation: AEL27767.1.
RefSeq	YP_004775998.1. NC_015914.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AEL27767; AEL27767; Cycma_4059.
GeneID	11036109.
KEGG	cmr:Cycma_4059.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K00820.
Enzyme and pathway databases
BioCyc	CMAR880070:GHDK-4103-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

G0J7R9_CYCMS

Accession

Primary (citable) accession number: G0J7R9

Entry history

Integrated into UniProtKB/TrEMBL:	October 19, 2011
Last sequence update:	October 19, 2011
Last modified:	April 3, 2013
This is version 14 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)