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Database: UniProt
Entry: A3DPP9_STAMF
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ID   A3DPP9_STAMF            Unreviewed;       608 AA.
AC   A3DPP9;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   OrderedLocusNames=Smar_1520 {ECO:0000313|EMBL:ABN70609.1};
OS   Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Staphylothermus.
OX   NCBI_TaxID=399550 {ECO:0000313|EMBL:ABN70609.1, ECO:0000313|Proteomes:UP000000254};
RN   [1] {ECO:0000313|Proteomes:UP000000254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1
RC   {ECO:0000313|Proteomes:UP000000254};
RX   PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA   Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA   Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA   Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA   Woese C., Bristow J., Kyrpides N.;
RT   "The complete genome sequence of Staphylothermus marinus reveals
RT   differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL   BMC Genomics 10:145-145(2009).
RN   [2] {ECO:0000313|EMBL:ABN70609.1, ECO:0000313|Proteomes:UP000000254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1
RC   {ECO:0000313|Proteomes:UP000000254};
RX   PubMed=21304655; DOI=10.4056/sigs.30527;
RA   Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT   type strain F1.";
RL   Stand. Genomic Sci. 1:183-188(2009).
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};
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DR   EMBL; CP000575; ABN70609.1; -; Genomic_DNA.
DR   RefSeq; WP_011839803.1; NC_009033.1.
DR   AlphaFoldDB; A3DPP9; -.
DR   STRING; 399550.Smar_1520; -.
DR   MEROPS; C44.A08; -.
DR   GeneID; 4906560; -.
DR   KEGG; smr:Smar_1520; -.
DR   eggNOG; arCOG00057; Archaea.
DR   HOGENOM; CLU_012520_7_0_2; -.
DR   OMA; THPLTDC; -.
DR   OrthoDB; 372195at2157; -.
DR   Proteomes; UP000000254; Chromosome.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
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   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR005855; GFAT.
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   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:ABN70609.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000254};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABN70609.1}.
FT   DOMAIN          2..223
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          287..428
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          458..599
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   608 AA;  67156 MW;  8E61FA6C41D41A2D CRC64;
     MGGIFGVVCK EKIRRGVVFE GLRRLLYRGY DGVGVAFLDD EGNIVIRKKP GHLEKVANEV
     DLFNIPSRIA LGHTRYASRG WPTVENTHPL TDCTGKIAVV GDGLIENYEA YKEKLVRKGH
     SFSSRTDTEV YAHLLEESVF REKKDPLEAI ARYMRELRGM YAVAAIIAGK EVFYVAHNGQ
     PLIIGLTHNN ECIYLSSDIP SLYGYADEAY ILEEGMAAEI SIDNIRIINA ENMEPISIER
     LIKKRVKYQV ELVGKAGYPH YMLKEIYEIP DSMIKTTYSL MEKYLRLAAM IIYGAKNVYV
     IGNGTSLHAG MVSSYYFTDL ANINVNVVSA AEFPYYALKN VSTGTVIIAI SQSGETSDVI
     KSVKLAKQYG AVIIGVTNVV GSRLSLESNV YLPIGAGPEL AVPATKTFVS SLVALALLAG
     YTGLYTGKLS QTEYVGITEK IRETAKELRK DLQVYDNIAE KISEKLLGWK NMYVSSSGIN
     YPVALEASLK FKEASIIHAE GVQLGELRHG PLVLIRDKYP VIIIKPVEEE ALPLYNKVAE
     YVLSKNGFLI TITHDDIGYG EVVKVKPTHK ILSPITTIIP LQLIAYHLGV KQGYPVDTPP
     GLAKAITT
//
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