GLMS_METMP
ID GLMS_METMP Reviewed; 599 AA.
AC Q6LWM9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE EC=2.6.1.16;
DE AltName: Full=D-fructose-6-phosphate amidotransferase;
DE AltName: Full=GFAT;
DE AltName: Full=Glucosamine-6-phosphate synthase;
DE AltName: Full=Hexosephosphate aminotransferase;
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase;
GN Name=glmS; OrderedLocusNames=MMP1680;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PH DEPENDENCE, AND SUBUNIT.
RC STRAIN=900;
RX PubMed=18263721; DOI=10.1128/jb.01970-07;
RA Namboori S.C., Graham D.E.;
RT "Acetamido sugar biosynthesis in the Euryarchaea.";
RL J. Bacteriol. 190:2987-2996(2008).
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000269|PubMed:18263721}.
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:0000269|PubMed:18263721};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active from pH 6.5 to 7.8. {ECO:0000269|PubMed:18263721};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18263721}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF31236.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX950229; CAF31236.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048064125.1; NC_005791.1.
DR AlphaFoldDB; Q6LWM9; -.
DR SMR; Q6LWM9; -.
DR STRING; 267377.MMP1680; -.
DR EnsemblBacteria; CAF31236; CAF31236; MMP1680.
DR GeneID; 2762284; -.
DR KEGG; mmp:MMP1680; -.
DR PATRIC; fig|267377.15.peg.1719; -.
DR eggNOG; arCOG00057; Archaea.
DR HOGENOM; CLU_012520_7_0_2; -.
DR OMA; ASEYRYA; -.
DR OrthoDB; 7487at2157; -.
DR BioCyc; MMAR267377:MMP_RS08650-MON; -.
DR Proteomes; UP000000590; 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; IDA:CACAO.
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; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR HAMAP; MF_00164; GlmS; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR005855; GlmS_trans.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01135; glmS; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Glutamine amidotransferase;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..599
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000333235"
FT DOMAIN 2..223
FT /note="Glutamine amidotransferase type-2"
FT DOMAIN 286..423
FT /note="SIS 1"
FT DOMAIN 452..589
FT /note="SIS 2"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 594
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 599 AA; 67138 MW; 872D121EDC1F106F CRC64;
MCGIIGYIGN EKASKILLKG LKRLEYRGYD SCGIATIDDT IKLKKNTGKV LEVSKKENFE
DMTGFIGIGH SRWATHGGIT KNNAHPHYDC SEKICIAHNG IISNYKELKE LLISKGHIFK
SETDTEVIPH LIEEEIKDFK EITEKTYINA IQNTIKKLNG TYALLILNQD FPEMLVGVRN
ESPLILGIKK DECFIGSDIS AFLEYTKLAM PLNDRDIVIL RKENDEIDIE VLNYGKQVQR
DTIELQWDME SAEKEGYEHF MLKEIMEEPV ILKNSMKISK LEIENLGKEI EKCDKIYITA
MGTSLHAAMV AEYWFSGLNK LVIPIDSSEF LTKGIVDEKT LVIAITQSGE TYDTMKAVKY
AKEKGAKTAT IVNVLGSTAT READITIMMG SGLEIAVCAT KTFMSQLVIL YRLFIEYGKI
IGKNMDIFEK ELLNIPNYIS KVLDEKENIS KIAEELTAKN YLFISKGINL ANALEGALKF
KEITYLHAEG MSSGFLKHGT ISLIDENMDT VALIPPSKSE LLNSVLSNVE EIKARNGKII
GISPVEDNLK YSIKVPDVIE EVSPFVYATA CQLLAYYKAV DLKRDVDKPR GLAKSVTVE
