ID A1RZ63_THEPD Unreviewed; 609 AA.
AC A1RZ63;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=Tpen_1094 {ECO:0000313|EMBL:ABL78493.1};
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL78493.1, ECO:0000313|Proteomes:UP000000641};
RN [1] {ECO:0000313|Proteomes:UP000000641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641};
RX PubMed=18263724; DOI=10.1128/JB.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
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; CP000505; ABL78493.1; -; Genomic_DNA.
DR RefSeq; WP_011752758.1; NC_008698.1.
DR AlphaFoldDB; A1RZ63; -.
DR STRING; 368408.Tpen_1094; -.
DR EnsemblBacteria; ABL78493; ABL78493; Tpen_1094.
DR GeneID; 4600961; -.
DR KEGG; tpe:Tpen_1094; -.
DR eggNOG; arCOG00057; Archaea.
DR HOGENOM; CLU_012520_7_0_2; -.
DR OrthoDB; 372195at2157; -.
DR Proteomes; UP000000641; 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 GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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 Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000313|EMBL:ABL78493.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000641};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..220
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 280..421
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 455..600
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 609 AA; 65060 MW; 28848B9080145633 CRC64;
MGGIFGAVSR SGGNVVPLVV TGLERLKYRG TDNSGIAVAR EGRLEVYKDT GPIDVVARKL
GLDKLQGSVA LGHTRYATHG RPTAENAHPH VDCGRRLAVV GDGSISNYEE LKDKVLLNGH
RLTSRSDFEV VAHVLEEAFR EGRAPEALPG VLSEKLQGFF AVAFLDASTG SIYAATTGPQ
LFLGASRELF LVSTSKYAMH GFAERYREVR RGEVVRVSSE GVEVYTGAGV GGLGELQPLH
LDPSLVEKNG YKHHMLREIY EVPESLMRTL SSVQKKYLQL AARLVTGADN VYIIANGTSL
HAGMVASYYF SELVGVNPVV VSAAEFPLYY LENIGPGSLV LAISQSGETG DVLSSLYEAK
LRGATILGIT NYVGSRLARL SNLYLPIAAG PELAVPATKT FTSTLLLLYL VALRASRQEG
RIDEDTLNSK LAAVAEAARQ LGEWLPKVDS EASKAANEVS ECRGGYVVSR GLTYPLALEG
ALKLKEASYF HAEGVEAGEF KHGPFVLVEK GFGVVFVVPV EKVSAEATYP LVGMALEAGA
KVVAVGFAGD QSLEALSEKG AAVVAAPPAE RHLAPIVLAV PLQLLAYRLG ERLSRPIDSP
RYLTKAVTQ
//