ID C1E1Z8_MICCC Unreviewed; 702 AA.
AC C1E1Z8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=MICPUN_93714 {ECO:0000313|EMBL:ACO61831.1};
OS Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO61831.1, ECO:0000313|Proteomes:UP000002009};
RN [1] {ECO:0000313|EMBL:ACO61831.1, ECO:0000313|Proteomes:UP000002009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
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};
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DR EMBL; CP001324; ACO61831.1; -; Genomic_DNA.
DR RefSeq; XP_002500573.1; XM_002500527.1.
DR AlphaFoldDB; C1E1Z8; -.
DR STRING; 296587.C1E1Z8; -.
DR GeneID; 8241764; -.
DR KEGG; mis:MICPUN_93714; -.
DR eggNOG; KOG1268; Eukaryota.
DR InParanoid; C1E1Z8; -.
DR OMA; ASEYRYA; -.
DR OrthoDB; 1705390at2759; -.
DR Proteomes; UP000002009; Chromosome 3.
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:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
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 InterPro; IPR017932; GATase_2_dom.
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 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 Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..284
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 377..516
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 548..692
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 220..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 77415 MW; 7719806AC21A5790 CRC64;
MCGIFAYVNY GVPTKQKAIV DKLLNGLRRL EYRGYDSAGI AIDNGPSLDE LSPIVLKETG
KIDMLADFIT NKENLNSDLF FENHCGIGHT RWATHGPPAP RNSHPHTSDA NNEFLVVHNG
IITNHQALRE MLERKGFVFE SETDTEVIPK LTKYLYEKFH NRVTFRQLVM EVVRQLQGAF
ALIFKSSHYP GELVAAKRGS PLLLGIVEEP GKNAPHAVLT SEGFKTSKEG PIGDEAPRDN
GGKRQKTLKN HVEYYFASDA SAMVEHTKRV LHLEDDDVAH LHNGGYGIYR MERSKPTSGT
SSPVHYEPTV QSAEVERTVE TLQMEVEQIM KGSFKHFMQK EIHEQPESMV QTMRGRMVTC
DEGKTAERVF LGGMVNFVST IRRSRRIILC GCGTSYNSAI AVRQLMEELT ELPVTLELAS
DVLDRQCPFF RDDTCVFISQ SGETADTLKA MQYAKERGAL CVGIVNTVGS AISRSTDCGV
HINAGAEIGV ASTKAYTCQI VAMVLLALAL SEDSISRATR RKEIMQSLLG LPEAVRTALK
LDAQMLALAE ALKDEQSLLL FGRGYNYATA LEGALKVKEV ALLHSEGILA GEMKHGPLAL
VDETMPLVVV ATRDGSYAKQ ESVVQQLRAR GGRLILIATE GDDQIAEVAG KDATIIWVPE
VEDCLQAVVN IVPLQLLSYH LTVLRGHNVD QPRNLAKSVT VE
//
