ID C7NS51_HALUD Unreviewed; 602 AA.
AC C7NS51;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=GFAT {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
GN Name=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN OrderedLocusNames=Huta_0471 {ECO:0000313|EMBL:ACV10658.1};
OS Halorhabdus utahensis (strain DSM 12940 / JCM 11049 / AX-2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=519442 {ECO:0000313|EMBL:ACV10658.1, ECO:0000313|Proteomes:UP000002071};
RN [1] {ECO:0000313|EMBL:ACV10658.1, ECO:0000313|Proteomes:UP000002071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12940 / JCM 11049 / AX-2
RC {ECO:0000313|Proteomes:UP000002071};
RX PubMed=21304660; DOI=10.4056/sigs.31864;
RA Anderson I., Tindall B.J., Pomrenke H., Goker M., Lapidus A., Nolan M.,
RA Copeland A., Glavina Del Rio T., Chen F., Tice H., Cheng J.F., Lucas S.,
RA Chertkov O., Bruce D., Brettin T., Detter J.C., Han C., Goodwin L.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Pitluck S., Pati A.,
RA Mavromatis K., Ivanova N., Ovchinnikova G., Chen A., Palaniappan K.,
RA Chain P., Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Halorhabdus utahensis type strain (AX-2).";
RL Stand. Genomic Sci. 1:218-225(2009).
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000256|HAMAP-Rule:MF_00164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001031, ECO:0000256|HAMAP-
CC Rule:MF_00164};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164}.
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DR EMBL; CP001687; ACV10658.1; -; Genomic_DNA.
DR RefSeq; WP_015788239.1; NC_013158.1.
DR AlphaFoldDB; C7NS51; -.
DR STRING; 519442.Huta_0471; -.
DR GeneID; 8382738; -.
DR KEGG; hut:Huta_0471; -.
DR eggNOG; arCOG00057; Archaea.
DR HOGENOM; CLU_012520_7_1_2; -.
DR OMA; GTSHYAG; -.
DR OrthoDB; 372195at2157; -.
DR Proteomes; UP000002071; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00714; GFAT; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_00164; GlmS; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR005855; GFAT.
DR InterPro; IPR047084; GFAT_N.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR NCBIfam; TIGR01135; glmS; 1.
DR PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00164};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000002071};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00164}.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT DOMAIN 2..218
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 283..422
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 453..592
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 597
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 602 AA; 63997 MW; 7DECB85E5E931F12 CRC64;
MCGITAQVGP TDAADTLLTC LENLEYRGYD SAGIALSDES GLTINKSEGT VGDLRAGISS
DTFDGGVGIG HTRWSTHGSP SDENAHPHTD CTGSIAVVHN GIIDNHEALR TELQSRGHEF
TSDTDTEVIP HLVSERLEAG EDIEAAFRGA VRELDGSYAV AMIVSGEQRV FATRHGSPLV
VGLGDRTQYL ASDVPAFIEY TDRVIYLEDG DVAVVGPSGH HVTDQAGKPV DRSVETVDWE
PEAAEKGGYD HYMLKEIQEQ PTSLRQTLEG RIREESVSLE SFPPGSFTDV STVQFVACGT
SYHAGLYGSH LLSEGGVPAT THLASEYAVY PPPIDEDTLV IAVTQSGETA DTLEALRVAK
EHGARTLAIT NVVGSTAARE SDDALLIRAG PEIGVAATKT FSSQVATLLL VANRLIEDVT
GELLDGHLDR LESLRSLPSF VQTGLDTSQA PAVADQYLSD GHFFIGRGNG VPVALEAALK
FKEITYEHAE GFPAGELKHG PLALVTADTP VFVVCTGRDA SKLESAIREV QTRGAPVIAV
APRSMSDIID TADETLTVPA THPDLVPILA NVQLQLVAYH AAAKLDRAID KPRNLAKSVT
VE
//