ID W6TSJ7_HOLOB Unreviewed; 593 AA.
AC W6TSJ7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 08-NOV-2023, entry version 40.
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=P618_201079 {ECO:0000313|EMBL:ETZ06787.1};
OS Holospora obtusa F1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales; Holosporaceae;
OC Holospora.
OX NCBI_TaxID=1399147 {ECO:0000313|EMBL:ETZ06787.1, ECO:0000313|Proteomes:UP000019112};
RN [1] {ECO:0000313|EMBL:ETZ06787.1, ECO:0000313|Proteomes:UP000019112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F1 {ECO:0000313|EMBL:ETZ06787.1,
RC ECO:0000313|Proteomes:UP000019112};
RX PubMed=25115770;
RA Dohra H., Tanaka K., Suzuki T., Fujishima M., Suzuki H.;
RT "Draft genome sequences of three Holospora species (Holospora obtusa,
RT Holospora undulata, and Holospora elegans), endonuclear symbiotic bacteria
RT of the ciliate Paramecium caudatum.";
RL FEMS Microbiol. Lett. 359:16-18(2014).
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:ETZ06787.1}.
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DR EMBL; AWTR02000085; ETZ06787.1; -; Genomic_DNA.
DR RefSeq; WP_021826816.1; NZ_AWTR02000085.1.
DR AlphaFoldDB; W6TSJ7; -.
DR STRING; 1399147.P618_201079; -.
DR eggNOG; COG0449; Bacteria.
DR Proteomes; UP000019112; 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; 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:ETZ06787.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000019112};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ETZ06787.1}.
FT DOMAIN 2..217
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 273..411
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 439..583
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 593 AA; 65263 MW; CF53D30EDB5F551D CRC64;
MCGIVGFIGK HPVLNVIVQA LKSVEYRGYD SSGIALVNQG HLVRYRSVGT LDQLVKILPT
NLSSTLGIGH TRWATHGAPE ERNAHPQVSR GVSVVHNGII ENFSELKSQL LKQGYTFESE
TDTEVVAHFI HLHYSKCKNI PELFSKILHD LEGSFALAIL LEDHSDHIFI ARKGVSPLTV
GRGPQGVSIG SDALSLVGIA EEICYIEDKT WGKLSLDKIE IFDTCQTPQP LHFILHPLGK
DALGRGEFAH YMLKEMYEQP EIVLKEGSRH LDIPEELTHA LHITLIGCGS AFYAAWGGKY
YLEHLAHRKA TLELASEFHY RNPIVQEGVT IAVSQSGETA DTLKAIQYME QKGQYTIGMV
NVPYSSIARQ VNYEILTNAG PEIGVASTKA FTAQLLCLLK ISISLMKDSA RKEKILNGLK
QLPLDMQKIF FKVSQLQDIA QHLVHAKGII FLGRGISYPV ALEGALKMSE LSYIFGQGFA
AGELKHGPLA LIDATTPVIV LAPMDQFFEK TVSNIYEVCA REGKVFIVTD EAGASQLAGV
PVQDIFVYPS PATWELHPFL SALSLQLIAY YTALHKGCSI DQPRNLAKSV TVE
//
