ID   GLMS_CYACA              Reviewed;         621 AA.
AC   O19908;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164};
DE            EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
GN   Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164}; Synonyms=gcaA;
OS   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC       fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00164};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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DR   EMBL; AF022186; AAB82681.1; -; Genomic_DNA.
DR   PIR; T11976; T11976.
DR   RefSeq; NP_045080.1; NC_001840.1.
DR   AlphaFoldDB; O19908; -.
DR   SMR; O19908; -.
DR   MEROPS; C44.A08; -.
DR   PRIDE; O19908; -.
DR   GeneID; 800239; -.
DR   GO; GO:0009507; C:chloroplast; 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; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
KW   Aminotransferase; Chloroplast; Glutamine amidotransferase; Plastid; Repeat;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   CHAIN           2..621
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000135421"
FT   DOMAIN          2..223
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          289..436
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          470..611
FT                   /note="SIS 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   ACT_SITE        616
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   621 AA;  69302 MW;  64718F4EBB9E8B69 CRC64;
     MCGIIGYVGE GSCRDVLING LDKLSYRGYD SAGIAFIKNS KINVVRSKGR IEKLKEKIND
     NFQKFEIGNI GIGHTRWATH GEPTEINAHP HLDAEGQFAV VQNGVIENYV QLKNYLTVNG
     TYFLSDTDAE VIPHLIAYKQ KHLKLQIVEA ILCALSELKG NFSTVIIARD MPDSIFVYQN
     KTALTLGKGS NFYSVSSDPI ALIPYTKNFI QLHDRELGII SISQLAIYNK GKFTYPSRRF
     KANLNDLITN KASFDSYTLK EIHDQKKVLR NLIISTLQSE KSIDESGQLH LEYKKIKNFQ
     IIACGSSFNA ALVGKVILEK LIRIPVHVYY GSEFKTNLPP LLPCTLTIAV SQSGETGDML
     SAIEIEKSRR KFQNTVYKPY LLSITNKNYS SITKKTAQSI DLKAGIEIGV AATKTFTAQT
     LSFYLLALKL AEHKFTLRKK EINKHLDEIR NLPKAIAHLL IKDESSIKWL SKQLKEISKC
     FYIGKGLNLG SALEGALKLK EISYIHCDGY AAGEIKHGPI ALVENNTLII TITDPEQSQE
     STFASSQEAK ARGAVLLAIT HIEDSSIYQT FDFIIKIPKI SQICASITSS VSLQLFAYYM
     AYYKGNDIDK PRNLAKSVTV E