ID A0RNJ2_CAMFF Unreviewed; 605 AA.
AC A0RNJ2;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 110.
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 {ECO:0000313|EMBL:ABK82470.1};
GN OrderedLocusNames=CFF8240_0586 {ECO:0000313|EMBL:ABK82470.1};
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106 {ECO:0000313|EMBL:ABK82470.1, ECO:0000313|Proteomes:UP000000760};
RN [1] {ECO:0000313|Proteomes:UP000000760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40 {ECO:0000313|Proteomes:UP000000760};
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) 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; CP000487; ABK82470.1; -; Genomic_DNA.
DR RefSeq; WP_002848996.1; NC_008599.1.
DR AlphaFoldDB; A0RNJ2; -.
DR MEROPS; C44.A08; -.
DR GeneID; 61064432; -.
DR KEGG; cff:CFF8240_0586; -.
DR eggNOG; COG0449; Bacteria.
DR HOGENOM; CLU_012520_5_2_7; -.
DR OMA; ASEYRYA; -.
DR Proteomes; UP000000760; 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; cd00714; GFAT; 1.
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; IPR047084; GFAT_N.
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:ABK82470.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000000760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABK82470.1}.
FT DOMAIN 2..221
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 284..424
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 457..595
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 605 AA; 67448 MW; F071409D3BC804A5 CRC64;
MCGIVGYIGD KEKKSIIING LKELEYRGYD SAGMAIMSGN CCSDINYFKS VGKLENLVSK
MESFTSKEFG VAIGHTRWAT HGKPTEINAH PHIGEYSFVI HNGIIENYKE LKDELETLGI
KFISQTDTEV IVHLFEYYNK TAQTPFDAYK KTISRLRGAY ATLLITKAAY GEIFFAKNAA
PLIIAKDGDE IYFSSSDAPL IGLAKDAMYL EDGSFGVAKL GEIKLFDKEA NELNLSFAPL
PKDKGYARKD GFRFFMEKEI YEQSQVITEC LMGRVGDDDI NLDIDNSIFD GIDEIVLCAC
GTSYHAALSA SYLFERVAKI RAKVEVASEF RYKEPLLRKS SLFIVISQSG ETADSLEALK
IAKNAGLKTM AICNVDNSSI VRLASEVILT RAGIEKGVAS TKAFATQVIC LWMLVLKLAK
LRQSIDTINL QNEIKALRNI PSVVHFDSSL QERIYRLAKH YLHGHGFFFI GRDIFYPLAL
EGALKLKEIS YLHAEGYPAG EMKHGPIALA DTGLYTIALL PKTLLYEKTK SNVEELAARD
AFITAISPEA FELSDDFIQT NLYDHPMSEF FEMMIVLQLF ALEISVRLGN DVDMPRNLAK
SVTVE
//