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
//