O57981 (GLMS_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	glmS
Ordered Locus Names:	PH0243

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › Pyrococcus horikoshii

Protein attributes

Sequence length	598 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.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Contains 1 glutamine amidotransferase type-2 domain. Contains 2 SIS domains.
Sequence caution	The sequence BAA29315.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Glutamine amidotransferase Repeat
Molecular function	Aminotransferase 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
	Chain	2 – 598	597	Glutamine--fructose-6-phosphate aminotransferase [isomerizing] HAMAP-Rule MF_00164		PRO_0000135431
Regions
	Domain	2 – 219	218	Glutamine amidotransferase type-2
	Domain	280 – 420	141	SIS 1
	Domain	449 – 588	140	SIS 2
Sites
	Active site	2	1	Nucleophile; for GATase activity By similarity
	Active site	593	1	For Fru-6P isomerization activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	O57981 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 3A8DD0466416544D	FASTA	598	66,110
	10 20 30 40 50 60 MCGIIGYIGP RKASDVIVEG LKRLEYRGYD SAGIATCYEG KIFIKKGAGK IDELVKKLNF 70 80 90 100 110 120 LELPGNIGIG HTRWATHGIP NDTNAHPHTD CTGKIVVVHN GIIENFQELK RELLKRGHVF 130 140 150 160 170 180 RSDTDTEVIA HLIEENLRIT GNFEDAFRMS LLRLRGSYAL VVLFADDPER LYIARKDSPL 190 200 210 220 230 240 IIGIGKGEMF MASDIPAFLA YTRRAVFLDD GEYGIVSKDW FTIKDIITGA VKTKEIHEIQ 250 260 270 280 290 300 WTLEMAEKGG YEHFMLKEIF EQPKAIKDAI YGNVKEAPKV AELLMKYDRI IITGMGTSYH 310 320 330 340 350 360 AALVGKYLIQ RFGKVPVIVE EASELRYEYE DILDNRSLLI AITQSGETAD TVAAMKLAKS 370 380 390 400 410 420 KGVEVVGIVN VVGSLATRIA DETLYTHAGP EIGVAATKTY TTQLVVLTLL AKELGKLVGI 430 440 450 460 470 480 DVSQIEGTIP RLPELVDSSL KINDKIREIA VKLNDKRDFF YIGRGINYPT ALEGALKIKE 490 500 510 520 530 540 IAYVHAEGLS AGELKHGPLA LIEDGIPVVG IAPTGKTFEK MLSNIEEAKA RGGFIISLGD 550 560 570 580 590 DVRLHQVSDI FIRLPKVPEE LAPITYIVPL QLLAYHLAVL KGHNPDRPRN LAKSVTVE

References

[1]

"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000001 Genomic DNA. Translation: BAA29315.1. Different initiation.
PIR	D71248.
RefSeq	NP_142239.1. NC_000961.1.
3D structure databases
ProteinModelPortal	O57981.
ModBase	Search...
Protein-protein interaction databases
STRING	70601.PH0243.
Proteomic databases
PRIDE	O57981.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA29315; BAA29315; BAA29315.
GeneID	1444133.
KEGG	pho:PH0243.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0449.
HOGENOM	HOG000258898.
KO	K00820.
OMA	CLQGLER.
ProtClustDB	PRK00331.
Enzyme and pathway databases
BioCyc	PHOR70601:GJWR-234-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

GLMS_PYRHO

Accession

Primary (citable) accession number: O57981

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program