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Database: UniProt
Entry: A0A0R2TZM1_9GAMM
LinkDB: A0A0R2TZM1_9GAMM
Original site: A0A0R2TZM1_9GAMM 
ID   A0A0R2TZM1_9GAMM        Unreviewed;       607 AA.
AC   A0A0R2TZM1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
DE   Flags: Fragment;
GN   ORFNames=ABS24_06865 {ECO:0000313|EMBL:KRO92567.1};
OS   SAR92 bacterium BACL26 MAG-121220-bin70.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae; SAR92 clade.
OX   NCBI_TaxID=1655626 {ECO:0000313|EMBL:KRO92567.1, ECO:0000313|Proteomes:UP000051213};
RN   [1] {ECO:0000313|EMBL:KRO92567.1, ECO:0000313|Proteomes:UP000051213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL26 MAG-121220-bin70 {ECO:0000313|EMBL:KRO92567.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) 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   -!- 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:KRO92567.1}.
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DR   EMBL; LICA01000322; KRO92567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2TZM1; -.
DR   Proteomes; UP000051213; 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:1901137; P:carbohydrate derivative biosynthetic 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   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,
KW   ECO:0000313|EMBL:KRO92567.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRO92567.1}.
FT   DOMAIN          2..218
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          286..426
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          458..599
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   NON_TER         607
FT                   /evidence="ECO:0000313|EMBL:KRO92567.1"
SQ   SEQUENCE   607 AA;  65868 MW;  21B0F96DE8FE7A7F CRC64;
     MCGIVGATAQ RNVYKILIEG LHRLEYRGYD SAGLSILDSD NSLQTRKTVG KVADLEAVCK
     DNFVSGNVGI SHTRWATHGA PSSINSHPHL SSGVSIVHNG IIENHDALRE ELRVAGYDIQ
     SDTDSEVIAH LVHQYLGSST DLRDAVNKTI ARLEGAYALG VISDEYPGLI VGARSGSPLV
     LGVGIDEHFI ASDQMALRQV TDRFVYLEEG DVVELSSETY TVFSANGKVV QRELHQLSDA
     DQVADKGQYR HFMQKEMFEQ ATVLANTFAG RIGKDHILEA IFGHQAEGLF AQTKNVHIIA
     CGTSFHSGLV AKYWLEDMAG VPCQVEVASE YRYRKVAVAE GTLFVSISQS GETADTLAAL
     HKAKKSGYLG FLAICNVANS SLVRESDISL MTMAGPEIGV ASTKAFTTQL VALQLLTLAL
     GRHTGLPPEV EAELVKNLHQ LPELCQRVLA LDSVIEKMAE AFANKHHALF LGRGEQYPIA
     LEGALKLKEI SYIHAEAYPA GELKHGPLAL VDEDMPVVTV APDNALLDKL KSNLHEVRAR
     GGQLFVFADC NANFKSEPGI TVIDMPPTPK SLEAIIYTLP LQMLSYHVAL LKGTDVDQPR
     NLAKSVT
//
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