ID B0WHH6_CULQU Unreviewed; 675 AA.
AC B0WHH6;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN Name=6038345 {ECO:0000313|EnsemblMetazoa:CPIJ006769-PA};
GN ORFNames=CpipJ_CPIJ006769 {ECO:0000313|EMBL:EDS27754.1},
GN CpipJ_CPIJ006770 {ECO:0000313|EMBL:EDS27755.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS27754.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS27754.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ006770-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ006769-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR EMBL; DS231936; EDS27754.1; -; Genomic_DNA.
DR EMBL; DS231936; EDS27755.1; -; Genomic_DNA.
DR RefSeq; XP_001848160.1; XM_001848108.1.
DR RefSeq; XP_001848161.1; XM_001848109.1.
DR AlphaFoldDB; B0WHH6; -.
DR STRING; 7176.B0WHH6; -.
DR EnsemblMetazoa; CPIJ006769-RA; CPIJ006769-PA; CPIJ006769.
DR EnsemblMetazoa; CPIJ006770-RA; CPIJ006770-PA; CPIJ006770.
DR GeneID; 6038345; -.
DR KEGG; cqu:CpipJ_CPIJ006769; -.
DR KEGG; cqu:CpipJ_CPIJ006770; -.
DR VEuPathDB; VectorBase:CPIJ006769; -.
DR VEuPathDB; VectorBase:CPIJ006770; -.
DR VEuPathDB; VectorBase:CQUJHB012155; -.
DR eggNOG; KOG1268; Eukaryota.
DR HOGENOM; CLU_012520_5_0_1; -.
DR InParanoid; B0WHH6; -.
DR OMA; ASEYRYA; -.
DR OrthoDB; 1705390at2759; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000002320; 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:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
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 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 4: Predicted;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:EDS27754.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDS27754.1}.
FT DOMAIN 2..281
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 353..493
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 524..665
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 675 AA; 75598 MW; 97ADB60FC4F6FE4E CRC64;
MCGIFAYLNY LTPKTRREVL DLLLTGLKRL EYRGYDSAGV AVDLPDQSGI AMFKRTGKVK
VLEEGIIEQT KDGSYDGTVE THVGISHTRW ATHGAPSEVN SHPQRSDDTN SFVVVHNGIV
TNYKDIKKFL ELRGYEFESD TDTETIAKLV HHLYIQHPNY SFRELVEQVV QQVEGAFALA
FKSKHFPGEC VVTRRGSPLL VGIKSTTSLA TNHVPILYGK GHRHGSNGNI QFEPTPDNTT
DFINPGEEVE YFFASDASAV IEHTNRVIYL EDDDVAAVKN GALGIHRLKK CLDDPHAREI
TTLKMEIQQI MKGNYRYFMQ KEIFEQPESV INTMRGRVNF ESMKVTLGGI KEYIPEIKRC
RRLMLIACGT SYHSAVATRQ LLEELTELPV MIELASDFLD RNTPIYRDDV CFFISQSGET
ADTLMALRYC KQRGALIVGV TNTVGSSICR ESHCGVHVNA GPEIGVASTK AYTSQFISLV
MFALVMSEDR LSLQTRREEI MEGLRQLDTH IKQVLKLDQK VLEIAQDLYQ QKSLLIMGRG
YNFATCMEGA LKVKELTYMH SEGIMAGELK HGPLALVDDT MPIVMIIMRD PVYVKCINAL
QQVTAREGRP IIVCEEGDAE TMSLASKALE IPRTVDCLQG ILTVIPMQLL SYHIAVLRGC
NVDCPRNLAK SVTVE
//
