ID Q5CS83_CRYPI Unreviewed; 696 AA.
AC Q5CS83;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 24-JAN-2024, entry version 82.
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=cgd1_3730 {ECO:0000313|EMBL:EAK88288.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK88288.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK88288.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
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:EAK88288.1}.
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DR EMBL; AAEE01000006; EAK88288.1; -; Genomic_DNA.
DR RefSeq; XP_628184.1; XM_628184.1.
DR AlphaFoldDB; Q5CS83; -.
DR STRING; 353152.Q5CS83; -.
DR MEROPS; C44.A08; -.
DR EnsemblProtists; EAK88288; EAK88288; cgd1_3730.
DR GeneID; 3371514; -.
DR KEGG; cpv:cgd1_3730; -.
DR VEuPathDB; CryptoDB:cgd1_3730; -.
DR InParanoid; Q5CS83; -.
DR OMA; ASEYRYA; -.
DR OrthoDB; 1705390at2759; -.
DR Proteomes; UP000006726; Chromosome 1.
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:EAK88288.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000006726};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAK88288.1}.
FT DOMAIN 84..307
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 373..512
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 545..686
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 696 AA; 76469 MW; 598A0E61446453C7 CRC64;
MNFSSKYKFL VPIVNRINDD LKEKNEKSKF YRFERLTKTM KDEQKLDFLR GSRIFGMISE
SIGSLCKTGR KNSIFSVPNK AYCCGIIGYI GSGDAQKVLM QGIEILQNRG YDSCGMSTID
DQGELITTKY SSKESGDSIE RLKNDSELLH GNHHIGIAHT RWATHGGKTD FNAHPHQDYK
KRISIVHNGT IDNYCSLKSE LMEKGIKFQS ETDTEVIANL IGSYLDDGED FQNAVQKALS
RLQGTWGIAV LHKDYKDLMI LARHGSPLLV GVQSGHIYIA SETSALANYT NQYVALQDGE
IALLSHEGIN KLITPSRLLS IDHEKVESSP SPYLHWTLKE IYDQPHALAR SLNFGGRISP
YNNMVKLGGL DQRLDELKNV QNMILLGCGT SFHAALFAQL LMEHISGFNT VSAKDASEIF
VTGFPREHAG AIAISQSGET ADTVKAINIA DKLGIPKISV VNVVGSMLAR TTGCGVYLNA
GREVAVASTK AFSTQVLVLS LIAAWFAQNR DSVISQRCQE LLEAIHRVPI SVGVSLQAKD
QCEQIAEMIK DNNSIFVLGK GYGYPVALEG ALKIKEISYI HSEGYSAGAL KHGPFALIDK
DSQTPVILVI LSDENQSLMM NVAQQVKARG ARVICITDDE NLCKDIDCEK VLIPSNGPLT
ALNAVIPLQL IAYYLAIKRG INPDKPRGLA KAVTVF
//
