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Database: UniProt
Entry: A0A0Q1A9M3_9BACT
LinkDB: A0A0Q1A9M3_9BACT
Original site: A0A0Q1A9M3_9BACT 
ID   A0A0Q1A9M3_9BACT        Unreviewed;       905 AA.
AC   A0A0Q1A9M3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   ORFNames=APR54_10460 {ECO:0000313|EMBL:KQC11871.1};
OS   Candidatus Cloacimonas sp. SDB.
OC   Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC   Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX   NCBI_TaxID=1732214 {ECO:0000313|EMBL:KQC11871.1, ECO:0000313|Proteomes:UP000052007};
RN   [1] {ECO:0000313|EMBL:KQC11871.1, ECO:0000313|Proteomes:UP000052007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDB {ECO:0000313|EMBL:KQC11871.1};
RA   Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA   Suflita J.M., Callaghan A.V.;
RT   "Methanogenic Paraffin-Utilizing Consortium.";
RL   Submitted (OCT-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:KQC11871.1}.
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DR   EMBL; LKUH01000022; KQC11871.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q1A9M3; -.
DR   Proteomes; UP000052007; 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:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
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; 1.
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; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:KQC11871.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQC11871.1}.
FT   DOMAIN          22..263
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          463..606
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   905 AA;  102622 MW;  4E09B4007345242B CRC64;
     MLLNSLIKLK LHLPIPVFGL GCGVLGMSLS KVSINLGKYA ATLLKALEYR GYDSTGAIFQ
     GDKQKIKLLK DVGAPSTLVK TLGIDNQPGR IFCGQVRWAT FGPVTPKNAQ PHEVKCKKHL
     YGAHNGNITN TTELKKFLLS QGHNIVSDND GEMLVHTIEH YFDIELVKFP VKQHRETAIR
     RECLQKAIIK SSDKVVGSYA AVVVDPVTEY SYAIKAGSSL YFGVGEVEDN KFTLASSDLT
     AVLKFTKQLV NLRQGEFIEF NKAEFQIYAL KKLRIKVPKS ETVTYNPGDK ISRISVRSRL
     RAEDTELKPP YKYFLEQEIH AEVESTGKLI KLFHGGSNTG KRMIRLLKKV DLLNKMTEIC
     NRIQATDDYA KQTKIFNEFE KSSDIEKFYT KIQTNYQAIY NELVKENFEK KYFFSSDKNI
     FIELLNSHFN KRKLLVAKAL DSITELDDVR EFNKSVENFL KMLQHTYNNS RNIYLVACGT
     SYHASLIAAL FFNEIANVDI IPVLPGNFRG LYSHSLRPDD IIIGISQSGE TKDLIDIFDH
     VDDQEMDIKK VVLLNNLNST LGQEKSDVTI PIYCGPEIAV PATKSFINQI TLFYYLAIKI
     AEKKLSDCTS KSSKKCLELE KRVKMRLNSL DFIPKLIKET LETTEEQIEF VTSKIYFEPS
     MHLLATKILG VAKEGALKIR ETLLNHAEGG EASEFKHGPN TILGKNTVFG IKNIRAMIKH
     YNENIDRMYI LADQKKVSSK ETRKISRAIS NYVFKQSYPF DLSPAAAELF EEVIKEFDFF
     ETAFRNYPLI YITGPEEKDV NLTISQINTH KIRGADTFVI AEENDDLLEN ARTNPHDEGY
     YGWGYITLPK TGDTLLTVFS ATIVLQLLAL RMSEKKMEKL DRLRISDHGV HPDVPKNVSK
     SITVD
//
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