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Database: UniProt
Entry: F7S5Q4_9PROT
LinkDB: F7S5Q4_9PROT
Original site: F7S5Q4_9PROT 
ID   F7S5Q4_9PROT            Unreviewed;       607 AA.
AC   F7S5Q4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
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   ORFNames=APM_1656 {ECO:0000313|EMBL:EGO95517.1};
OS   Acidiphilium sp. PM.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=1043206 {ECO:0000313|EMBL:EGO95517.1, ECO:0000313|Proteomes:UP000004823};
RN   [1] {ECO:0000313|EMBL:EGO95517.1, ECO:0000313|Proteomes:UP000004823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM {ECO:0000313|EMBL:EGO95517.1,
RC   ECO:0000313|Proteomes:UP000004823};
RX   PubMed=21914891; DOI=10.1128/JB.05386-11;
RA   San Martin-Uriz P., Gomez M.J., Arcas A., Bargiela R., Amils R.;
RT   "Draft Genome Sequence of the Electricigen Acidiphilium sp. Strain PM (DSM
RT   24941).";
RL   J. Bacteriol. 193:5585-5586(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}.
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:EGO95517.1}.
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DR   EMBL; AFPR01000160; EGO95517.1; -; Genomic_DNA.
DR   RefSeq; WP_007422810.1; NZ_AFPR01000160.1.
DR   AlphaFoldDB; F7S5Q4; -.
DR   HOGENOM; CLU_012520_5_2_5; -.
DR   Proteomes; UP000004823; Unassembled WGS sequence.
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   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..217
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          283..422
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          455..597
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        602
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   607 AA;  64092 MW;  DA320C7D6BB9FF78 CRC64;
     MCGIVGLIGR NDAAPLLLDG LSRLAYRGYD SAGIATLVEG AITRRRAEGK LANLAASLAA
     APLAGTTGIG HTRWATHGAP TEGNAHPHGT ARVAVVHNGI IENHAELRAE LEAAGQVFST
     ETDTETVAQL VDLHLARGLA PVEAAAAAFA RLEGAYALAL IFAGHPELII GAQRGAPLAV
     GFGEEEMYLG SDALALAPLT RRIAYLDDGD WVIVSRSGAE FRDAANNPVA REVKLTRLTG
     ASIGKGNFRH FMEKELHENP AIIGDTLNRM IDPATRLPVL PDLAVDLAAI PRITLSACGS
     AYYAGLTARY WLEEIARIAV DADVASEFRY REPPLDPAGL GLVISQSGET ADTMAALRYM
     KRQGCKVMSV VNVPESTMAR ESDLMLETIA GPEISVASTK AFTAQLAVLA GFTLALARAR
     GARSDAEIAP LVAALMELPG KMAQLLADDT EIRALAEDIR DARDVLFFGR GSMMPIALEG
     ALKLKELSYI HAEGYPAGEM KHGPIALIDP SVPVIAVLPS GPLFEKTASN LQEAAARGGR
     IILFSDKAGA ARLAGIANRT IIITECDPFV APILYAIPVQ LLAYHVAVLK GTDVDQPRNL
     AKSVTVE
//
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