ID G8LRV2_9FLAO Unreviewed; 612 AA.
AC G8LRV2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 08-NOV-2023, entry version 61.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090, ECO:0000256|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916, 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 ECO:0000313|EMBL:AEU09325.1};
GN ORFNames=BLBCPU_271 {ECO:0000313|EMBL:AEU09325.1};
OS Blattabacterium sp. (Cryptocercus punctulatus) str. Cpu.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=1075399 {ECO:0000313|EMBL:AEU09325.1, ECO:0000313|Proteomes:UP000007112};
RN [1] {ECO:0000313|EMBL:AEU09325.1, ECO:0000313|Proteomes:UP000007112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cpu {ECO:0000313|EMBL:AEU09325.1,
RC ECO:0000313|Proteomes:UP000007112};
RX PubMed=22094859;
RA Neef A., Latorre A., Pereto J., Silva F.J., Pignatelli M., Moya A.;
RT "Genome economization in the endosymbiont of the wood roach Cryptocercus
RT punctulatus due to drastic loss of amino acid synthesis capabilities.";
RL Genome Biol. Evol. 3:1437-1448(2011).
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; CP003015; AEU09325.1; -; Genomic_DNA.
DR RefSeq; WP_014246213.1; NC_016621.1.
DR AlphaFoldDB; G8LRV2; -.
DR STRING; 1075399.BLBCPU_271; -.
DR KEGG; bcp:BLBCPU_271; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_10; -.
DR Proteomes; UP000007112; 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}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
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 289..428
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 461..602
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 607
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 612 AA; 68675 MW; 3535B3383DC91F5F CRC64;
MCGIIGYLGY REAYPIIING LKKLEYRGYD SSGIAIFYNG KYSLYKTKGR VSELEKKIFS
IKGTTGIGHT RWATHGIPDD INAHPHVSNS KKLVLIHNGI IENYHAIKII LLKNGFTFQS
ETDTEVLVNL IEYIQKKNQL SLEEAVRISL NEVIGAYSIA VIEKSDPDRI VIAKLGSPLT
LGINEKEFFI ASDPIPFIDY TKNAIYLKDG EMAILRKNKE LDLRKIIDNH KLNPIIKELK
INLKEIEKGE YKHFMLKEIY EQPKTILDTL RGRLLISDGL ICIDGIESNK DIFINAKCIT
IVACGTSWHS SLIGEYLLEE LARIPVKVEY ASEFRYRNPI IEKQNIVIVI SQSGETADTI
AALKLAKKKG AFVFGICNVA GSYIARNVDA GAYTHAGPEI GVASTKSFTS QITVLFLLAL
KIGKHRSTIT NIRYEFLCKE LISVPEKMNF TLKIDNTLQK ISKLYHHVNN FLYLGRGINF
PVSLEGALKL KEISYIHAEG YPAGEMKHGP IALIDENMPV VVIATKKGYY EKIIGNIQEI
KARKGKIIAI VNERDIQVSK LADHIIEIPI ISEELSPLIT IIPLQLLAYQ IADLRGKNVD
RPRNLAKSVT VE
//