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Database: UniProt
Entry: A0A075K7F3_9FIRM
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ID   A0A075K7F3_9FIRM        Unreviewed;       609 AA.
AC   A0A075K7F3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=UFO1_0626 {ECO:0000313|EMBL:AIF50181.1};
OS   Pelosinus sp. UFO1.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF50181.1, ECO:0000313|Proteomes:UP000027983};
RN   [1] {ECO:0000313|EMBL:AIF50181.1, ECO:0000313|Proteomes:UP000027983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UFO1 {ECO:0000313|EMBL:AIF50181.1};
RX   PubMed=25189589;
RA   Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L.,
RA   Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.;
RT   "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using
RT   Single-Molecule Real-Time DNA Sequencing Technology.";
RL   Genome Announc. 2:e00881-14(2014).
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; CP008852; AIF50181.1; -; Genomic_DNA.
DR   RefSeq; WP_038667886.1; NZ_CP008852.1.
DR   AlphaFoldDB; A0A075K7F3; -.
DR   STRING; 484770.UFO1_0626; -.
DR   KEGG; puf:UFO1_0626; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_5_2_9; -.
DR   OrthoDB; 106547at2; -.
DR   Proteomes; UP000027983; 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:UP000027983};
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          286..425
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          454..599
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        604
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   609 AA;  67060 MW;  9640F4F5A887382E CRC64;
     MCGIVGYIGP KQASTFLIEG LSKLEYRGYD SAGIAVYDGT QVHVEKSVGR LANLEKKLDN
     EQLIGNLGIG HTRWATHGRP SDVNSHPHTD CTGDFVVVHN GIIENYMHLK EKLIAKGHVF
     TSETDTEVVA HLVEEHYKGD FEAAVKKVLS EIEGSYALVF MTKHEPDKII CTKQDNPLVI
     GLGEGENFIA SDIPAIINRT RKTYILSDGE LAVVTKDSVW VMNRQGVPIT KKVFEVNWDA
     EAAEKGGYEH FMIKEIYEQP KAIRETMSSR LAKDDSHIIL DELKWTKHEI AAIKKVVIVA
     CGTAYHAGIV GKYYIESLAR IPVEVDVASE FRYRSPLVDE NTLAIVVSQS GETLDTLAAL
     KEAKRLGAKT LAITNVVGSS ISREADQVIY TWAGPEIAVA STKAYTTQLV SMAMLAIYIA
     GLRENISAER SRELISGLRN LPAQLHEILE DVESIKTFAQ QYGFNEDVFF IGRSLDYAVA
     LEGALKLKEI SYIHAEAYAA GELKHGTLAL IIEGVPVIAL ATQHDVYDKT LSNIKEVKAR
     DAVVIGIAQQ GDDQINKYVD HAIFIPQADK FLAPILAVIP LQLLAYYAAI TRGCDVDKPR
     NLAKSVTVE
//
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