ID A0A9D4B1R6_9SAUR Unreviewed; 976 AA.
AC A0A9D4B1R6;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 9.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN ORFNames=KIL84_011211 {ECO:0000313|EMBL:KAH1177509.1};
OS Mauremys mutica (yellowpond turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Geoemydidae; Geoemydinae; Mauremys.
OX NCBI_TaxID=74926 {ECO:0000313|EMBL:KAH1177509.1, ECO:0000313|Proteomes:UP000827986};
RN [1] {ECO:0000313|EMBL:KAH1177509.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MM-2020 {ECO:0000313|EMBL:KAH1177509.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAH1177509.1};
RA Gong S., Gao Y.;
RT "The genome of Mauremys mutica provides insights into the evolution of
RT semi-aquatic lifestyle.";
RL Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC fructose 6-phosphate: step 1/1. {ECO:0000256|ARBA:ARBA00004775}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAH1177509.1}.
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DR EMBL; JAHDVG010000474; KAH1177509.1; -; Genomic_DNA.
DR Proteomes; UP000827986; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:InterPro.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:TreeGrafter.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:TreeGrafter.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:TreeGrafter.
DR CDD; cd00714; GFAT; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR FunFam; 3.40.50.10490:FF:000001; Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; 1.
DR FunFam; 3.40.50.10490:FF:000126; Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1; 1.
DR FunFam; 3.30.1370.70:FF:000002; NFU1 iron-sulfur cluster scaffold homolog, mitochondrial; 1.
DR Gene3D; 3.40.50.10490; Glucose-6-phosphate isomerase like protein, domain 1; 2.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 3.30.1370.70; Scaffold protein Nfu/NifU, N-terminal domain; 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; IPR014824; Nfu/NifU_N.
DR InterPro; IPR036498; Nfu/NifU_N_sf.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR NCBIfam; TIGR01135; glmS; 1.
DR NCBIfam; NF001484; PRK00331.1; 1.
DR PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR PANTHER; PTHR10937:SF12; GLUTAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE [ISOMERIZING] 1; 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF08712; Nfu_N; 1.
DR Pfam; PF01380; SIS; 2.
DR SMART; SM00932; Nfu_N; 1.
DR SUPFAM; SSF110836; Hypothetical protein SAV1430; 1.
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 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000827986};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 279..582
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 654..793
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 825..966
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 175..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..220
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..253
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 107974 MW; EAB9E9A19016F552 CRC64;
MAAAARWLRA AAGLGGRFCR MTLKDFNLTT KQPLCQFVRR KPFLPSTVAH NTVRCMFIQT
QDTPNPNSLK FIPGRQVLES RTMDFSTPAA AFCSPLARQL FRIEGVKSVF FGPDFITVTK
VSEDWDWNLL KPDIYATIMD FFASGLPVIT EEAPRTDTGG AGSWPHLAAD AFPVPNPPLS
APLVPPPPFH SPSPPPPSGA DADPDPACHV PSATAPLRAG PAGGAGRRGP GPMAGSARSL
RPWAPACPAP GRCPARKSGP RRPAEQSWAG LSPGAGTMCG IFAYLNYHVP RTRREILETL
IKGLQRLEYR GYDSAGVGID GGNDKDWEAN AGKIQLIKKK GKVKALDEEI NKQQDMDLDI
EFDVHLGIAH TRWATHGEPS PVNSHPQRSD KNNEFIVIHN GIITNYKDLR KFLESKGYDF
ESETDTETIA KLVKYMYDNR ESDDISFTTL VERVIQQLEG AFALVFKSVH YHGQAVGTRR
GSPLLIGVRS EHKLSTDHIP ILYRTAVQSM DHSVGGISIE AEKGKDKKGS CSLSRIDSTT
CLFPVEEKAV EYYFASDASA VIEHTNRVIF LEDDDVAAVV DGRLSIHRIK RTAGDHPGRA
VQTLQMELQQ IMKGNFSSFM QKEIFEQPES VVNTMRGRVN FDDYTVNLGG LKDHIKEIQR
CRRLILIACG TSYHAGVATR QVLEELTELP VMVELASDFL DRNTPVFRDD VCFFISQSGE
TADTLMGLRY CKERGALTVG ITNTVGSSIS RETDCGVHIN AGPEIGVAST KAYTSQFVSL
VMFALMMCDD RISMQERRKE IMRGLKVLPD LIKEVLSMDD EIQKLATELY HQKSVLIMGR
GYHYATCLEG ALKIKEITYM HSEGIMAGEL KHGPLALVDK LMPVIMIIMR DHTYAKCQNA
LQQVIARQGR PVVICDKEDT ETINNNKRTI KVPHSVDCLQ GILSVIPLQL LAFHLAVLRG
YDVDFPRNLA KSVTVE
//
