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Database: UniProt
Entry: A4A977_9GAMM
LinkDB: A4A977_9GAMM
Original site: A4A977_9GAMM 
ID   A4A977_9GAMM            Unreviewed;       609 AA.
AC   A4A977;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 2.
DT   24-JAN-2024, entry version 91.
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   ORFNames=KT71_04900 {ECO:0000313|EMBL:EAQ97619.2};
OS   Congregibacter litoralis KT71.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Congregibacter.
OX   NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ97619.2, ECO:0000313|Proteomes:UP000019205};
RN   [1] {ECO:0000313|EMBL:EAQ97619.2, ECO:0000313|Proteomes:UP000019205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT71 {ECO:0000313|EMBL:EAQ97619.2,
RC   ECO:0000313|Proteomes:UP000019205};
RX   PubMed=17299055; DOI=10.1073/pnas.0608046104;
RA   Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., Schattenhofer M.,
RA   Yan S., Ferriera S., Johnson J., Glockner F.O., Amann R.;
RT   "Characterization of a marine gammaproteobacterium capable of aerobic
RT   anoxygenic photosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007).
RN   [2] {ECO:0000313|EMBL:EAQ97619.2, ECO:0000313|Proteomes:UP000019205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT71 {ECO:0000313|EMBL:EAQ97619.2,
RC   ECO:0000313|Proteomes:UP000019205};
RX   PubMed=19287491; DOI=10.1371/journal.pone.0004866;
RA   Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.;
RT   "The photosynthetic apparatus and its regulation in the aerobic
RT   gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov.";
RL   PLoS ONE 4:E4866-E4866(2009).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAQ97619.2}.
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DR   EMBL; AAOA02000002; EAQ97619.2; -; Genomic_DNA.
DR   RefSeq; WP_023659766.1; NZ_CM002299.1.
DR   AlphaFoldDB; A4A977; -.
DR   STRING; 314285.KT71_04900; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_5_2_6; -.
DR   OrthoDB; 9761808at2; -.
DR   Proteomes; UP000019205; 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:UP000019205};
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..219
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          286..426
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          458..599
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        604
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   609 AA;  65857 MW;  24586D2E56FA068B CRC64;
     MCGIVAATAR REVSEILLEG LRRLEYRGYD SAGMALIDNE QRLQLHKYQG KVAALEEAQT
     LNPILGCTGI AHTRWATHGQ PSAANAHPHI SGQRIAVVHN GIIENHKALR EELSDAGYDF
     VSATDTEVIV HLLHKSVSEG NTLLEAMRST VSLLEGAYAL AAIDTHSPEE VVAARSGSPL
     VVGVGIGEHF LASDTMALRQ VTDRFIYLDE GDVVVCSAAG LAIYDDAGEP VQREMKKISG
     DVEDADLGDF EHYMLKEIYE QPHALAATFA KALDQKVDDS VFGDAAAEVF AKTRAVQIVA
     CGTSYHAGLV ARYWLEDIAG IPCQVEVASE FRYRKRVAHP GTLLVTISQS GETADTLAAL
     RHAEPGEFVA SLVIANVDNS SLVRESDMAF LTRAGIEIGV ASTKAFTTQL VAFLMLALVL
     GRHRGLSPER EQLLLDGLAQ LPELVKQTLK IDPQIEAMSA AFIQKHHALF LGRGIQYPIA
     MEGALKLKEI SYIHAEAYPA GELKHGPLAL VDADMPIVAV APNDDLLDKL KSNLEEVRSR
     GGELYVFADG SAGFKDEPGV HVLAMPHTPE ILQPVIYTVA LQLLAYHVAL QKGTDVDKPR
     NLAKSVTVE
//
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