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Database: UniProt
Entry: GLMS_MYCTU
LinkDB: GLMS_MYCTU
Original site: GLMS_MYCTU 
ID   GLMS_MYCTU              Reviewed;         624 AA.
AC   P9WN49; L0TCI8; O06253; O33274; P0A588;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   08-NOV-2023, entry version 49.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164};
DE            EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
GN   Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164}; OrderedLocusNames=Rv3436c;
GN   ORFNames=MTCY77.08c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RA   Schaeffer M.L., Besra G.S., Belisle J.T., Inamine J.M.;
RT   "Biochemical and genetic definition of effects of mannosamine on
RT   mycobacteria.";
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Mckendree W.L., Schuster S.M., Richards N.;
RT   "Structure of a recombinant glmS protein from Mycobacterium tuberculosis
RT   expressed in E. coli.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011445;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(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:0000255|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:0000255|HAMAP-Rule:MF_00164};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA04007.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF002814; AAB69988.1; -; Genomic_DNA.
DR   EMBL; AJ000333; CAA04007.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL123456; CCP46258.1; -; Genomic_DNA.
DR   PIR; B70976; B70976.
DR   RefSeq; NP_217953.1; NC_000962.3.
DR   RefSeq; WP_003418289.1; NZ_NVQJ01000027.1.
DR   AlphaFoldDB; P9WN49; -.
DR   SMR; P9WN49; -.
DR   STRING; 83332.Rv3436c; -.
DR   PaxDb; 83332-Rv3436c; -.
DR   DNASU; 887568; -.
DR   GeneID; 887568; -.
DR   KEGG; mtu:Rv3436c; -.
DR   TubercuList; Rv3436c; -.
DR   eggNOG; COG0449; Bacteria.
DR   InParanoid; P9WN49; -.
DR   OMA; ASEYRYA; -.
DR   OrthoDB; 9761808at2; -.
DR   PhylomeDB; P9WN49; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
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:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
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   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:0000255|HAMAP-Rule:MF_00164"
FT   CHAIN           2..624
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000135357"
FT   DOMAIN          2..225
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          297..436
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          469..614
FT                   /note="SIS 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   ACT_SITE        619
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   624 AA;  67572 MW;  ABDFAE5F55549916 CRC64;
     MCGIVGYVGR RPAYVVVMDA LRRMEYRGYD SSGIALVDGG TLTVRRRAGR LANLEEAVAE
     MPSTALSGTT GLGHTRWATH GRPTDRNAHP HRDAAGKIAV VHNGIIENFA VLRRELETAG
     VEFASDTDTE VAAHLVARAY RHGETADDFV GSVLAVLRRL EGHFTLVFAN ADDPGTLVAA
     RRSTPLVLGI GDNEMFVGSD VAAFIEHTRE AVELGQDQAV VITADGYRIS DFDGNDGLQA
     GRDFRPFHID WDLAAAEKGG YEYFMLKEIA EQPAAVADTL LGHFVGGRIV LDEQRLSDQE
     LREIDKVFVV ACGTAYHSGL LAKYAIEHWT RLPVEVELAS EFRYRDPVLD RSTLVVAISQ
     SGETADTLEA VRHAKEQKAK VLAICNTNGS QIPRECDAVL YTRAGPEIGV ASTKTFLAQI
     AANYLLGLAL AQARGTKYPD EVEREYHELE AMPDLVARVI AATGPVAELA HRFAQSSTVL
     FLGRHVGYPV ALEGALKLKE LAYMHAEGFA AGELKHGPIA LIEDGLPVIV VMPSPKGSAT
     LHAKLLSNIR EIQTRGAVTI VIAEEGDETV RPYADHLIEI PAVSTLLQPL LSTIPLQVFA
     ASVARARGYD VDKPRNLAKS VTVE
//
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