ID A8MC94_CALMQ Unreviewed; 595 AA.
AC A8MC94;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=Cmaq_0557 {ECO:0000313|EMBL:ABW01400.1};
OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS IC-167).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=397948 {ECO:0000313|EMBL:ABW01400.1, ECO:0000313|Proteomes:UP000001137};
RN [1] {ECO:0000313|EMBL:ABW01400.1, ECO:0000313|Proteomes:UP000001137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167
RC {ECO:0000313|Proteomes:UP000001137};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Caldivirga maquilingensis IC-167.";
RL Submitted (OCT-2007) 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};
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DR EMBL; CP000852; ABW01400.1; -; Genomic_DNA.
DR RefSeq; WP_012185620.1; NC_009954.1.
DR AlphaFoldDB; A8MC94; -.
DR STRING; 397948.Cmaq_0557; -.
DR GeneID; 5709019; -.
DR KEGG; cma:Cmaq_0557; -.
DR eggNOG; arCOG00057; Archaea.
DR HOGENOM; CLU_012520_7_0_2; -.
DR OrthoDB; 372195at2157; -.
DR Proteomes; UP000001137; 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:ABW01400.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001137};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABW01400.1}.
FT DOMAIN 2..218
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 280..424
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 446..586
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 595 AA; 65307 MW; 3CD418982F086F02 CRC64;
MGGIFGLVSN IRPVAPVIRI GLERLMHRGI DGAGIATVYN SVIHIKKDAG KVTDVHSKLN
LDDLPGYVGI GHVRSATHGR PVYENTHPVQ DCTGGVALVM DGVVSDYDEI RRRLSRRHKL
VSRTDAEALA HIIEDELKDG KSMREALSSV TRQVKGYYTI AVLNKDEERI YALSMGNPLV
IGVSDREYFV SSEEQAIPVK LRLVYFMEPN QMVVMSKDGV EFYDASSMSK VEPSPQLASQ
TTVEVVKGSF QHYMIKEIYE EPEVLARAVN VLQREYLDDA ASIVAKAKNI IFTGSGTSYY
ASLIGKYYLE ELGGVKADAI PAGEFPYLGV RYVEPGTLII AISQSGESTD IIRTIRWAKR
KGAIVLSIVN RLGSALMRES NVYLPMGAGP ELAVPATKSF VASIAIMLQL AYAVKGNVND
ARSLINKAII MLNNQINKVR DDVRRIAKLV SNYNNAYIIS GGPIGLPLAM EAALKLKEAA
QVHSEAFSFR EFKHGPITLI SKEFPTIAIM PGNDVDDEII NVISEVWSRG GYTVVITQEG
KEVTGDQVIY LERMGNRLII PLVYPAVIQL LAYEIGVARG IDVDNPHNLS KVVTT
//
