ID D7CJ00_SYNLT Unreviewed; 606 AA.
AC D7CJ00;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 80.
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=Slip_2135 {ECO:0000313|EMBL:ADI02878.1};
OS Syntrophothermus lipocalidus (strain DSM 12680 / TGB-C1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophothermus.
OX NCBI_TaxID=643648 {ECO:0000313|EMBL:ADI02878.1, ECO:0000313|Proteomes:UP000000378};
RN [1] {ECO:0000313|Proteomes:UP000000378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX DOI=10.4056/sigs.1233249;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Djao O., Zhang X., Lucas S., Lapidus A., Glavina Del Rio T., Nolan M.,
RA Tice H., Cheng J., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA Jeffries C., Rohde M., Sikorski J., Spring S., Goker M., Detter J.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT C1T).";
RL Stand. Genomic Sci. 3:267-275(2010).
RN [2] {ECO:0000313|EMBL:ADI02878.1, ECO:0000313|Proteomes:UP000000378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX PubMed=21304731;
RA Djao O.D., Zhang X., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Rohde M., Sikorski J., Spring S., Goker M., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT C1).";
RL Stand. Genomic Sci. 3:268-275(2010).
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; CP002048; ADI02878.1; -; Genomic_DNA.
DR RefSeq; WP_013176280.1; NC_014220.1.
DR AlphaFoldDB; D7CJ00; -.
DR STRING; 643648.Slip_2135; -.
DR KEGG; slp:Slip_2135; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_9; -.
DR OMA; ASEYRYA; -.
DR OrthoDB; 106547at2; -.
DR Proteomes; UP000000378; 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:UP000000378};
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..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; 66167 MW; A62A8E55CCDC328D CRC64;
MCGITGYIGS NQAVPVIIDG LKRLEYRGYD SAGIAVIQEE RLWLLKKEGR LERLEGILNG
SHPTSGLGIG HTRWATHGVP SDDNAHPHTD CQGRIAVVHN GIIENFASLR RWLEREGHRF
SSETDTEVLA HLVEHHYHGS LEEAVRRALE AVEGSYALAV ICADEPDKIV AVRNQSPLVI
GVGENEYYLA SDIPAILNRT RKVYLLEDRE MAVLTRDGVA ISNGEGKRVA KDMFTVTWSA
EAAEKGGYPH FMIKEIMEQP QALRDTLRGR IQGGRVEFSD VDLDCCLDGV EKVFIVACGT
AYHAGVVGKH VIERLACLPV EVDIASEFRY RDVLWGDKSL LIVISQSGET ADTLAALREA
KKKGIRVLAV TNVVGSSVAR EADRVIYTWA GPEIAVASTK AYSTQLLVMY LLGLYLAQKR
GTLPEEVIAS TVRELRGIAD KVEAILEKAG AVEAIAEKYA ATASTFFIGR GLDYAVALEG
ALKLKEISYV HAEAYAAGEL KHGTLALIEK GVPVIAIVTQ DELQDKMISN IKEVKARGAE
VIGIAKEGLA GIEEETDELF VIPGEDSLLT PMLTVVPLQL FAYYMAVKRG CDVDKPRNLA
KSVTVE
//