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Database: UniProt
Entry: D3SSJ5_NATMM
LinkDB: D3SSJ5_NATMM
Original site: D3SSJ5_NATMM 
ID   D3SSJ5_NATMM            Unreviewed;       602 AA.
AC   D3SSJ5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164};
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=glmS3 {ECO:0000313|EMBL:ADD06840.1};
GN   Synonyms=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN   OrderedLocusNames=Nmag_3290 {ECO:0000313|EMBL:ADD06840.1};
GN   ORFNames=C500_13781 {ECO:0000313|EMBL:ELY28232.1};
OS   Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS   IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS   magadii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=547559 {ECO:0000313|EMBL:ADD06840.1, ECO:0000313|Proteomes:UP000001879};
RN   [1] {ECO:0000313|Proteomes:UP000001879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC   8861 / NBRC 102185 / NCIMB 2190 / MS3
RC   {ECO:0000313|Proteomes:UP000001879};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E.,
RA   Maupin-Furlow J.A., Woyke T.;
RT   "Complete sequence of chromosome of Natrialba magadii ATCC 43099.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADD06840.1, ECO:0000313|Proteomes:UP000001879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD06840.1}, and ATCC 43099 / DSM
RC   3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861 / NBRC 102185 /
RC   NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000001879};
RX   PubMed=22559199; DOI=10.1186/1471-2164-13-165;
RA   Siddaramappa S., Challacombe J.F., Decastro R.E., Pfeiffer F., Sastre D.E.,
RA   Gimenez M.I., Paggi R.A., Detter J.C., Davenport K.W., Goodwin L.A.,
RA   Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., Maupin-Furlow J.A.;
RT   "A comparative genomics perspective on the genetic content of the
RT   alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T.";
RL   BMC Genomics 13:165-165(2012).
RN   [3] {ECO:0000313|EMBL:ELY28232.1, ECO:0000313|Proteomes:UP000011543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC   8861 / NBRC 102185 / NCIMB 2190 / MS3
RC   {ECO:0000313|Proteomes:UP000011543}, and MS-3
RC   {ECO:0000313|EMBL:ELY28232.1};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [4] {ECO:0000313|EMBL:ADD06840.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD06840.1};
RA   Pfeiffer F.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001932; ADD06840.1; -; Genomic_DNA.
DR   EMBL; AOHS01000043; ELY28232.1; -; Genomic_DNA.
DR   RefSeq; WP_004215940.1; NZ_AOHS01000043.1.
DR   AlphaFoldDB; D3SSJ5; -.
DR   STRING; 547559.Nmag_3290; -.
DR   PaxDb; 547559-Nmag_3290; -.
DR   GeneID; 8826154; -.
DR   KEGG; nmg:Nmag_3290; -.
DR   PATRIC; fig|547559.17.peg.2727; -.
DR   eggNOG; arCOG00057; Archaea.
DR   HOGENOM; CLU_012520_7_1_2; -.
DR   OMA; RECALQF; -.
DR   OrthoDB; 372195at2157; -.
DR   Proteomes; UP000001879; Chromosome.
DR   Proteomes; UP000011543; Unassembled WGS sequence.
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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00164};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001879};
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..217
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          282..420
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          453..592
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   REGION          55..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT   ACT_SITE        597
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   602 AA;  64543 MW;  44D411F544E59CB4 CRC64;
     MCGIIARIGQ GEAADTLLTG LENLEYRGYD SAGIAVQNGS GVKVHKCSGE VSELKSQLDG
     QPHGNLGIGH TRWSTHGPPT DENAHPHTDT VGDVAVVHNG VIDNYDDLKA DLQAKGHEFE
     SDTDTEVIPH LINEYLDNVD DTEIAVRQAV DTLEGSYAIA AIVDGEERVY AARKGSPLVL
     GLDDEEWYLA SDVPAFLDHT DEVIYLEDGD LVTLEPDSYW ITDLEGQPVD REVDTVDWDP
     EDAGKGEYDH YMLKEIHNQP TSLSNTIEGR ADDGDVAFED LPAGTFAEIE TVQFVACGTS
     YHAAMYGAQL LREAGLRTEV VRASEYDATA GPVDENTLVV AVTQSGETAD TLDAVRTATD
     RGARSLAVTN VVGSTISREA DDAVYIRAGP EVGVAATKTF SSQAVTLSLL TQRIAADVPE
     ATPAADRDAM LAELQHLPEY VEQVLESTRA ETLAEETLDS DSYFFIGNGL GHSVALEGAL
     KFKEITYEHA EGFASGQLKH GPLALVTEAS PIFAVVTGDG DEKTKTNAIE AQSRGAPIVA
     VGPEEHALVD VADEHLSVPA THPVWAGLLA NVQLQLVSYH AAELLDRPID KPRNLAKSVT
     VE
//
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