ID F2I1N3_PELSM Unreviewed; 606 AA.
AC F2I1N3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090, ECO:0000256|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916, ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=GFAT {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
GN Name=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN OrderedLocusNames=SAR11G3_01272 {ECO:0000313|EMBL:AEA81747.1};
OS Pelagibacter sp. (strain IMCC9063).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=1002672 {ECO:0000313|EMBL:AEA81747.1, ECO:0000313|Proteomes:UP000009181};
RN [1] {ECO:0000313|EMBL:AEA81747.1, ECO:0000313|Proteomes:UP000009181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC9063 {ECO:0000313|EMBL:AEA81747.1,
RC ECO:0000313|Proteomes:UP000009181};
RX PubMed=21515764; DOI=10.1128/JB.05033-11;
RA Oh H.M., Kang I., Lee K., Jang Y., Lim S.I., Cho J.C.;
RT "Complete genome sequence of strain IMCC9063, belonging to SAR11 subgroup
RT 3, isolated from the Arctic Ocean.";
RL J. Bacteriol. 193:3379-3380(2011).
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000256|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:0000256|ARBA:ARBA00001031, ECO:0000256|HAMAP-
CC Rule:MF_00164};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164}.
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DR EMBL; CP002511; AEA81747.1; -; Genomic_DNA.
DR RefSeq; WP_013695912.1; NC_015380.1.
DR AlphaFoldDB; F2I1N3; -.
DR STRING; 1002672.SAR11G3_01272; -.
DR KEGG; pel:SAR11G3_01272; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_5; -.
DR OrthoDB; 9761808at2; -.
DR Proteomes; UP000009181; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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; 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, ECO:0000256|HAMAP-
KW Rule:MF_00164}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000009181};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00164}.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT DOMAIN 2..216
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 282..421
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 454..596
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 601
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 606 AA; 67546 MW; 879FE54FE1A7FA15 CRC64;
MCGIIGIASS KPVVSNIISS LKKLEYRGYD SAGIATFSNN FIDEIKCEGR VNKLEKICSK
KTFAGIVGIG HVRWATHGIP NEINAHPHSN ESVSVVHNGI IENSTILKKL LEKKGYKFKS
QTDTEVITAL LSENLKKNTP LVAIQKTLEK LHGSYALGIL FKDNPDLIVG ARRGSPLAVG
YGHNENYLGS DSYALKSMTN KISYLEDGEI CLLTKDNAEF YNSKGKKINK KILTLSEESE
SYEKGDFKTF MQKEIFEQPD TAKSCINEYV DHLRDDINIY NLPWDIQKID SITLIGCGTA
YHACMIAKYW LEELTSLDVV IDIASEFRYK TNKFKKNNLY IFVSQSGETA DTFAALELCK
KNKMKTLSIV NVVESSIARN SDLVLPIHCG AEIGVASTKA FTGQMLVLYI LTLKISFLKK
DINKKTFEQK IKELKKLPKL IKSTLSVESE IENISNTFAN AKGSMFLGRG FAYPVAMEGA
LKLKELCYVH AEGYPAGEMK HGPLALIEEG IPVVVLAPRD KYYEKTLSNM QEVISRGAKV
LLISNKSKDE ISSENVWKTI EVEKTSDELL PFLLTLPLQI LAFHSAKNKG YDIDKPRNLA
KSVTVE
//
