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Database: UniProt
Entry: F1ZDM4_9SPHN
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Original site: F1ZDM4_9SPHN 
ID   F1ZDM4_9SPHN            Unreviewed;       607 AA.
AC   F1ZDM4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
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=Y88_3702 {ECO:0000313|EMBL:EGD57392.1};
OS   Novosphingobium nitrogenifigens DSM 19370.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=983920 {ECO:0000313|EMBL:EGD57392.1, ECO:0000313|Proteomes:UP000004728};
RN   [1] {ECO:0000313|EMBL:EGD57392.1, ECO:0000313|Proteomes:UP000004728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19370 {ECO:0000313|EMBL:EGD57392.1,
RC   ECO:0000313|Proteomes:UP000004728};
RX   PubMed=22156397; DOI=10.1128/JB.06381-11;
RA   Strabala T.J., Macdonald L., Liu V., Smit A.M.;
RT   "Draft Genome Sequence of Novosphingobium nitrogenifigens Y88T.";
RL   J. Bacteriol. 194:201-201(2012).
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:EGD57392.1}.
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DR   EMBL; AEWJ01000065; EGD57392.1; -; Genomic_DNA.
DR   RefSeq; WP_008071502.1; NZ_GL876935.1.
DR   AlphaFoldDB; F1ZDM4; -.
DR   STRING; 983920.Y88_3702; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_5_2_5; -.
DR   InParanoid; F1ZDM4; -.
DR   OrthoDB; 9761808at2; -.
DR   Proteomes; UP000004728; 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}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004728};
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          283..422
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          455..597
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        602
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   607 AA;  65279 MW;  8EC8B58ECEE5D6DD CRC64;
     MCGIIGIVGK EQVADRLVDG LRRMEYRGYD SAGVCTIDHG ELIRRRAEGK LANLVTELAR
     NPAPGLVGIA HTRWATHGAP TTNNAHPHAT GEVALVHNGI IENFRPLREE LIARGRTFES
     ETDTEVVAHL VSEQVEAGLS PEDAVKVVLP RLRGAFALAI AFRSHPDILI GARLGSPLVV
     GYGEGEMFLG SDALALAPLT QRVSYLEEGD WVVISREGAQ VFDVHNTPVK RAVVASGATA
     AAIEKGNYRH FMQKEIYEQP IVVAQTLRSY LRRYEQVVSL PQIDFDLASI RRVTIVACGT
     SYYAGMVAKY WFERFARLPV DIDVASEFRY RDPVLEPGGL ALFISQSGET ADTLAALRHC
     KAAGQTIAVV VNVPTSSMAR EADLLLPTHA GPEIGVASTK AFTCQLAVLA ALAVHLAVKR
     GLITHEEEAQ IVDQLVETPA ALNAALAHDE EIAAMAPLIA PARDVLYLGR GPDYPLALEG
     ALKLKEISYI HAEGYASGEM KHGPIALIDE QVPVIVLAPS GPLFEKTVSN MQEVRARGGK
     IVLISDAEGL AEAGEGCLAT IEMPKVHPLI APLVYAVPVQ LLAYHVAVAK GTDVDQPRNL
     AKSVTVE
//
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