ID A0A136L200_9CHLR Unreviewed; 517 AA.
AC A0A136L200;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN Name=glmS_1 {ECO:0000313|EMBL:KXK15752.1};
GN ORFNames=UZ14_CFX002000339 {ECO:0000313|EMBL:KXK15752.1};
OS Chloroflexi bacterium OLB14.
OC Bacteria; Chloroflexota; Tepidiformia.
OX NCBI_TaxID=1617415 {ECO:0000313|EMBL:KXK15752.1, ECO:0000313|Proteomes:UP000070321};
RN [1] {ECO:0000313|EMBL:KXK15752.1, ECO:0000313|Proteomes:UP000070321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB14 {ECO:0000313|EMBL:KXK15752.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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};
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:KXK15752.1}.
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DR EMBL; LMZR01000011; KXK15752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136L200; -.
DR STRING; 1617415.UZ14_CFX002000339; -.
DR PATRIC; fig|1617415.3.peg.344; -.
DR Proteomes; UP000070321; Unassembled WGS sequence.
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 ECO:0000313|EMBL:KXK15752.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXK15752.1}.
FT DOMAIN 1..125
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 193..333
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 366..507
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 517 AA; 56732 MW; ECD60993AA9D1AED CRC64;
MVHNGIVENF LELKDELSSE GVIFNSDTDT ETIVHLAEHH HAAGISFTEA ARRTFKQIEG
ANVVLLMSTD EPDKIVTARI GNAGGVVIGL GENENYIASD IPAILEHTRK VIFLESKQMA
IVTRDSVRIE TLDGVEIKPE IHTINWDAVS AEKGEYRHFM QKEIHEQVRA LTDTLAGRVD
FKEGRIRLPE LKLTPELAKK IQRIYITACG TAAYAGMVGK YLIEKIARIP VEVVIGSEFR
YSDPIVDENT VVLAISQSGE TADTLAAMEE GKRKGGIVWS IVNAVGSQAM RVADGYIAMQ
TGPEIGVAST KAFTAPLVDQ YMLAILLADL RGVIDEQTRK QLVSDLRLVP DLAGRALDAE
SQIEKVAQAL KDIKGCLYLG RGINMPIAYE GALKLKEISY IHAEGYPAGE MKHGPIALID
EEMPVICIAP KDPWHEKMIS QIQQAKARGG MVVAVATEGD ELIKEMADHV LWIPEAPWML
SPIITVLPLQ LLAYHIATTR GLDVDQPRNL AKSVTVE
//
