ID I7ISJ5_BABMR Unreviewed; 670 AA.
AC I7ISJ5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN ORFNames=BmR1_04g07400 {ECO:0000313|EMBL:CCF75671.1};
OS Babesia microti (strain RI).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=1133968 {ECO:0000313|EMBL:CCF75671.1, ECO:0000313|Proteomes:UP000002899};
RN [1] {ECO:0000313|EMBL:CCF75671.1, ECO:0000313|Proteomes:UP000002899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RI {ECO:0000313|EMBL:CCF75671.1,
RC ECO:0000313|Proteomes:UP000002899};
RX PubMed=22833609; DOI=10.1093/nar/gks700;
RA Cornillot E., Hadj-Kaddour K., Dassouli A., Noel B., Ranwez V.,
RA Vacherie B., Augagneur Y., Bres V., Duclos A., Randazzo S., Carcy B.,
RA Debierre-Grockiego F., Delbecq S., Moubri-Menage K., Shams-Eldin H.,
RA Usmani-Brown S., Bringaud F., Wincker P., Vivares C.P., Schwarz R.T.,
RA Schetters T.P., Krause P.J., Gorenflot A., Berry V., Barbe V.,
RA Ben Mamoun C.;
RT "Sequencing of the smallest Apicomplexan genome from the human pathogen
RT Babesia microti.";
RL Nucleic Acids Res. 40:9102-9114(2012).
RN [2] {ECO:0000313|EMBL:CCF75671.1, ECO:0000313|Proteomes:UP000002899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RI {ECO:0000313|EMBL:CCF75671.1,
RC ECO:0000313|Proteomes:UP000002899};
RX PubMed=24023759; DOI=10.1371/journal.pone.0072657;
RA Cornillot E., Dassouli A., Garg A., Pachikara N., Randazzo S., Depoix D.,
RA Carcy B., Delbecq S., Frutos R., Silva J.C., Sutton R., Krause P.J.,
RA Mamoun C.B.;
RT "Whole genome mapping and re-organization of the nuclear and mitochondrial
RT genomes of Babesia microti isolates.";
RL PLoS ONE 8:e72657-e72657(2013).
RN [3] {ECO:0000313|EMBL:CCF75671.1, ECO:0000313|Proteomes:UP000002899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RI {ECO:0000313|EMBL:CCF75671.1,
RC ECO:0000313|Proteomes:UP000002899};
RX PubMed=27752055; DOI=10.1038/srep35284;
RA Silva J.C., Cornillot E., McCracken C., Usmani-Brown S., Dwivedi A.,
RA Ifeonu O.O., Crabtree J., Gotia H.T., Virji A.Z., Reynes C., Colinge J.,
RA Kumar V., Lawres L., Pazzi J.E., Pablo J.V., Hung C., Brancato J.,
RA Kumari P., Orvis J., Tretina K., Chibucos M., Ott S., Sadzewicz L.,
RA Sengamalay N., Shetty A.C., Su Q., Tallon L., Fraser C.M., Frutos R.,
RA Molina D.M., Krause P.J., Ben Mamoun C.;
RT "Genome-wide diversity and gene expression profiling of Babesia microti
RT isolates identify polymorphic genes that mediate host-pathogen
RT interactions.";
RL Sci. Rep. 6:35284-35284(2016).
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; LN871599; CCF75671.1; -; Genomic_DNA.
DR RefSeq; XP_012650079.1; XM_012794625.1.
DR AlphaFoldDB; I7ISJ5; -.
DR GeneID; 24426123; -.
DR KEGG; bmic:BmR1_04g07400; -.
DR VEuPathDB; PiroplasmaDB:BmR1_04g07400; -.
DR OrthoDB; 1705390at2759; -.
DR Proteomes; UP000002899; Chromosome iv.
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 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; 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 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:CCF75671.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000002899};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCF75671.1}.
FT DOMAIN 40..275
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 328..482
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 516..660
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 670 AA; 74101 MW; 253C65A113CDE7FD CRC64;
MDENRKGGVL NYIRCLSTNL YSTVSPWIRL RSLIPRTECC GIVGASGFDD VQVYLYQGIE
YLQHRGYDSC GIATRKDDGS LVITKCSGNS SVPNKQSNPI ECLSRLKDLA SNNHLKSRTG
IGHTRWATVG GLNDKNAHPH SDYKNRIALA HNGTIYNSHW LFEHLKCSPL FPKIKLPESD
SEAVAHLIGM EMDSGLELED AINSTIKKLD GTWAFVIAST ALPYLIVSRK ESPLLIGKRN
DDNGVIVASE VIAFGSGVDK YVPLSDNTTM KLDDATMDKL FSTGPVYQIN NPKFETSPSP
YKYWIEKEIY EQPKRLQDLF NNQNFNSILQ SISNEPGIGK FDFIFAGCGS SLHSAHFIAY
IMKLLIHKSA KNTFKVYVVD TSEMTKESAM EFYGSPKFII YLSQSGETLD TIHSFNLLKT
ISPKSITISI VNDCNSYLAQ ITNYPLCLNA GREMSVASTK TFTSQSFAGL KLIQSIVSQL
SMPDSQKITS ALESSLSLLP TSITSVCNQV EKIQKLAKQI TTICETCNSL FILGRGAYFV
IAKEGALKLK EVPYLHAEAV QSGLMKHGTL AMINSKDKTP TISLIFEEDY SVPICAAEQL
KARGSYVVCV TDKKELVEDF ADEFIVIKDI GYATPLSAVV VFQLLAYFCA MERGIDPDYP
RGLAKTVTVL
//
