ID Q4UFR7_THEAN Unreviewed; 802 AA.
AC Q4UFR7;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=TA15930 {ECO:0000313|EMBL:CAI74049.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI74049.1, ECO:0000313|Proteomes:UP000001950};
RN [1] {ECO:0000313|EMBL:CAI74049.1, ECO:0000313|Proteomes:UP000001950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR940348; CAI74049.1; -; Genomic_DNA.
DR RefSeq; XP_951781.1; XM_946688.1.
DR AlphaFoldDB; Q4UFR7; -.
DR STRING; 5874.Q4UFR7; -.
DR GeneID; 3861871; -.
DR KEGG; tan:TA15930; -.
DR VEuPathDB; PiroplasmaDB:TA15930; -.
DR eggNOG; KOG1268; Eukaryota.
DR InParanoid; Q4UFR7; -.
DR OMA; GCTAKYW; -.
DR OrthoDB; 1705390at2759; -.
DR Proteomes; UP000001950; Chromosome 2.
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:CAI74049.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000001950};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAI74049.1}.
FT DOMAIN 35..299
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 428..569
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 653..792
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 176..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 89647 MW; 3D9FD32D6751E21F CRC64;
MNFATKFLDF LSIKKSKNDN DTCYIKKKGF YTYCCGIVGY LGNEDTNEIL LHGINAMKSR
GYDSCGVCTL HKGKLKVTKC CSVETPADSF NILKDKVLSS HPPSTVGIGH TRWATVGKLS
NKNSHPHIDL AKNIALVHNG TISNIEDLYH DYYAELISQK NKFSFGGSKY HSINKNIGNS
ANSTPTTKES SDETQQNAFQ LPDSDSESVA IFVGLEYENT GDLLLAFKNT IKKLKGTWAL
CMMSQHYPNS LFVAAHEAPL LVARSERGVY VGSEPNVFMK YVKDCIVLND GDILELSLEN
VESYYSQYNL LKLESEVVEE TCEPYPNWYT KEILEQIYIG RIIISLLSEQ SNFLYQFSFD
DMAPIGNQQN QNQVMNEEAN ELLSLRDKYL GNDNLCVIEG DPNHDNSLLS KVDISTFGFD
FPNLPQDILI RLKKTKKLLF VACGSSLHAA TYVAKILQKI HHFDLVEVDD ASDLTLYRYH
DKDVTVVHIS NSGETLDCIL ALNFIKRINP DCLSISIINT VHTSLERSSD ATIHLRIGRE
KSVPSTKAFT AQVTVLLIFS LYIISNNEII LDPLDDSTDY CSSVDKDEPS EYLELTNKDF
SEQLTTDEDE DETYNEHYGS CHNYTIASLY KSLSIFPSAI AKLLKNDEQY DSLAQWLLKE
KIVYILGRGC GHVVALEASL KMKEVAYIQA EGVLSGAMKH GIYAMIKEEE NTTTISIITS
EDKEMTINST LQIKARGGYI IVITDLEDEV DFADVLIRIP SIGALTPALA IIPIQIITSK
IAILSNRNPD IPRGLAKTVT TL
//
