GLMS_METJA
ID GLMS_METJA Reviewed; 1099 AA.
AC Q58815;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 148.
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;
DE Contains:
DE RecName: Full=Mja gf6p intein;
GN Name=glmS; OrderedLocusNames=MJ1420;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the SIS family. GFAT
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB99430.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L77117; AAB99430.1; ALT_INIT; Genomic_DNA.
DR PIR; C64477; C64477.
DR AlphaFoldDB; Q58815; -.
DR SMR; Q58815; -.
DR STRING; 243232.MJ_1420; -.
DR EnsemblBacteria; AAB99430; AAB99430; MJ_1420.
DR KEGG; mja:MJ_1420; -.
DR eggNOG; arCOG00057; Archaea.
DR eggNOG; arCOG01863; Archaea.
DR eggNOG; arCOG03151; Archaea.
DR HOGENOM; CLU_285704_0_0_2; -.
DR InParanoid; Q58815; -.
DR OMA; NSRWATH; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR CDD; cd00093; HTH_XRE; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR Gene3D; 3.10.28.10; -; 1.
DR Gene3D; 3.60.20.10; -; 2.
DR InterPro; IPR001387; Cro/C1-type_HTH.
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; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
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; PF13537; GATase_7; 1.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF14528; LAGLIDADG_3; 2.
DR Pfam; PF01380; SIS; 2.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
DR SUPFAM; SSF56235; SSF56235; 2.
DR TIGRFAMs; TIGR01135; glmS; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS51464; SIS; 2.
PE 3: Inferred from homology;
KW Aminotransferase; Autocatalytic cleavage; Cytoplasm; DNA-binding;
KW Glutamine amidotransferase; Protein splicing; Reference proteome; Repeat;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..71
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing], 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010848"
FT CHAIN 72..570
FT /note="Mja gf6p intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010849"
FT CHAIN 571..1099
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing], 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010850"
FT DOMAIN 2..71
FT /note="Glutamine amidotransferase type-2; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 198..253
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DOMAIN 278..413
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT DOMAIN 571..723
FT /note="Glutamine amidotransferase type-2; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 786..923
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 948..1089
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 1094
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1099 AA; 125501 MW; A4CFE30CB3894F16 CRC64;
MCGIIGYIGN DKAPKILLNG LRRLEYRGYD SCGIGVVDNN KLIIKKNVGK VEEVAKKERF
LDIDGNIGIG HCLHPDTYVI LPDGRMKKIS EIDEDEVLSV NFEDLKLYNK KIKKFKHKAP
KILYKIKTAF SELITTGEHK LFVVENGKIV EKCVKDLNGS ELIGVVRKLN YSFNDNVEFK
DVYVERHYKL DETIRNKLRK VREKLGLTRK DVEKLCGVKE IYIVKIETGK LESIEEERLK
KLCSLYGINF EEIIYRDNLH YTNPVKFPKT PTPELMQIIG YIIGDGHFPS NRMLRLKDER
KEVLEEYNQL FKTVFNLEGN IKKGDGNYYI LEINSKYLID WFRENIPELF NKTGNERTPE
FVFRLNNDLV ASYLRGIFDA EGYIRAEAKQ IGIGMTSKCF IKEIQFLLLR FGILASYSKI
KRKEENWNNT HKLLISDKKS FELFKKYIGF TAKDKMEKLE AILNKMKGLN FRYISIPLTK
KEIREFVGVP LKTIKNGDNY CTDYTIEKII EELNSKGLYD KAEYLKRFLD ADIVWTKFKI
EEVESDVEYV YDLEVEDYHN FIGNLIINHN SRWATHGNVC KENAHPHTDC KEEIAVVHNG
IISNYKELKD ELMKKGHKFK SETDTEVVPH LIEEELKKFK EINEENYIKA VKNAIKKLKG
TYALVIINKN FPNLLIGARN ESPLILGIND DGYFLGSDIT AFLDYTNKAI PLEDGDVVVI
KKKENGYEVT IENNGNTVER EMMEINWDIS SAEKMGYPHF MLKEIMEQPE VLKVSAKISA
EEIKELAKCI KDYDRVYFVA MGTSLHAAMV VEYLFAKLGK LVIACDASEF LNKGVVDDKT
LVIGITQSGE TYDTLKALRF AKKNKAKTGA IVNVLGSTAT READITVMMG AGIEIAVCAT
KTYTSQLMIL YRLFIEYGKL LGRDMSEYEK EIDKIPNYIK EVLDKKETIK EIANNLKVNN
YIFISKGINI ASALEGALKF KEITYLHAEG MSGGLLKHGT ISLIDENMDT VAIVPPRDSA
VFNSILSNIE EVKARGGKVI AITPTEIDGA ENILVPEVIE EISPIVYAPA FQLLAYYKAV
ELGRDVDKPR GLAKSVTVE
