(data stored in ACNUC1104 zone)

SWISSPROT: D3UXZ6_XENBS

ID   D3UXZ6_XENBS            Unreviewed;       609 AA.
AC   D3UXZ6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164, ECO:0000256|SAAS:SAAS00887593};
DE            EC=2.6.1.16 {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   ECO:0000313|EMBL:CBJ79174.1};
GN   OrderedLocusNames=XBJ1_0019 {ECO:0000313|EMBL:CBJ79174.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79174.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79174.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79174.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism,
CC       converting fructose-6P into glucosamine-6P using glutamine as a
CC       nitrogen source. {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,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725,
CC         ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={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,
CC       ECO:0000256|SAAS:SAAS00887591}.
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DR   EMBL; FN667741; CBJ79174.1; -; Genomic_DNA.
DR   RefSeq; WP_012986647.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0019; -.
DR   EnsemblBacteria; CBJ79174; CBJ79174; XBJ1_0019.
DR   GeneID; 8829646; -.
DR   KEGG; xbo:XBJ1_0019; -.
DR   PATRIC; fig|406818.4.peg.15; -.
DR   eggNOG; ENOG4105C46; Bacteria.
DR   eggNOG; COG0449; LUCA.
DR   HOGENOM; HOG000258898; -.
DR   KO; K00820; -.
DR   OMA; ASEYRYA; -.
DR   BioCyc; XBOV406818:XBJ1_RS00075-MONOMER; -.
DR   Proteomes; UP000002045; 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   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.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
DR   PRODOM; D3UXZ6.
DR   SWISS-2DPAGE; D3UXZ6.
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000313|EMBL:CBJ79174.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000256|SAAS:SAAS00887588};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000313|EMBL:CBJ79174.1}.
FT   INIT_MET      1      1       Removed. {ECO:0000256|HAMAP-Rule:
FT                                MF_00164}.
FT   DOMAIN        2    218       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   DOMAIN      286    426       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   DOMAIN      458    599       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   ACT_SITE      2      2       Nucleophile; for GATase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00164}.
FT   ACT_SITE    604    604       For Fru-6P isomerization activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00164}.
SQ   SEQUENCE   609 AA;  66806 MW;  4C6C0A4159C0D14B CRC64;
     MCGIVGAVAQ RDIAEILIEG LRRLEYRGYD SAGLAVVDSE NGMTRLREVG KVQMLADEAG
     KQPVTGGTGI AHTRWATHGE PNELNAHPHV SEHIAVVHNG IIENYEELRE LLKERGYTFF
     SDTDTETIAH LVHWEQKQGG SLLEVVQRVI PQLRGAYGTV IMDSRHPDVL VAARSGSPLV
     IGLGVGENFL ASDQLALLPV TRRFIYLEEG DIVEITRRTV RIFDVTGAAV EREQIESNVQ
     YDAGDKGIYR HYMQKEIYEQ PMAIKSTLEG RLSHGQVDLS ELGANAEELL SQVEHIQIVA
     CGTSYNAGMV SRYWFESLAG IPCDVEIASE FRYRKPARRK GSLLITLSQS GETADTLAAL
     RLSKELGYLT SLVICNVAGS SLVRESDFAL MTKAGAEIGV ASTKAFTTQL TVLLMLVAYM
     GRLKGADAAL EQDVVHALQA LPSRIESMLS KDKVIEALAE DFSEKHHALF LGRGDQYPIA
     VEGALKLKEI SYIHAEAYAA GELKHGPLAL IDADMPVIIV APNNELLEKL KSNIEEVRAR
     GGQLYVFADQ DAGFTNSENM KIISLPHVED LIAPIFYTVP LQLLSYHVAL IKGTDVDQPR
     NLAKSVTVE
//

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