GFA1_SCHPO
ID GFA1_SCHPO Reviewed; 696 AA.
AC Q09740;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE Short=GFAT;
DE EC=2.6.1.16;
DE AltName: Full=D-fructose-6-phosphate amidotransferase;
DE AltName: Full=Hexosephosphate aminotransferase;
GN ORFNames=SPBC12C2.11, SPBC21D10.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Involved in amino sugar synthesis (formation of chitin,
CC supplies the amino sugars of asparagine-linked oligosaccharides of
CC glycoproteins). {ECO:0000250}.
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 -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC fructose 6-phosphate: step 1/1.
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DR EMBL; CU329671; CAA20758.1; -; Genomic_DNA.
DR PIR; T11674; T11674.
DR RefSeq; NP_596011.1; NM_001021919.2.
DR AlphaFoldDB; Q09740; -.
DR SMR; Q09740; -.
DR BioGRID; 276179; 1.
DR STRING; 4896.SPBC12C2.11.1; -.
DR iPTMnet; Q09740; -.
DR MaxQB; Q09740; -.
DR PaxDb; Q09740; -.
DR PRIDE; Q09740; -.
DR EnsemblFungi; SPBC12C2.11.1; SPBC12C2.11.1:pep; SPBC12C2.11.
DR GeneID; 2539622; -.
DR KEGG; spo:SPBC12C2.11; -.
DR PomBase; SPBC12C2.11; -.
DR VEuPathDB; FungiDB:SPBC12C2.11; -.
DR eggNOG; KOG1268; Eukaryota.
DR HOGENOM; CLU_012520_5_2_1; -.
DR InParanoid; Q09740; -.
DR OMA; ASEYRYA; -.
DR PhylomeDB; Q09740; -.
DR Reactome; R-SPO-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00113; UER00528.
DR PRO; PR:Q09740; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; ISO:PomBase.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR005855; GlmS_trans.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 3: Inferred from homology;
KW Aminotransferase; Glutamine amidotransferase; Reference proteome; Repeat;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..696
FT /note="Probable glutamine--fructose-6-phosphate
FT aminotransferase [isomerizing]"
FT /id="PRO_0000135288"
FT DOMAIN 2..303
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 375..514
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 547..686
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 696 AA; 77322 MW; 9C4867168FB3EBFA CRC64;
MCGIFGYINY LVERDRGYIL KTLVKGLKRL EYRGYDSSGC AVDGDEGEDF IMFKEVGNVS
KLEASIKGSN VNKSTKFINH CAISHTRWAT HGIPSPINCH PQRSDPHSEF IVVHNGILTN
YRELRTVLES RGMVFESETD TECVAKLAKF IYDTTPGVDF TSLAKLVFRE LEGAYALLIK
SSHYPGEVVA TRRGSPLIVG VKSEQKLKVD FVDVEFPEPA EGLPGTPKPT SLHPVFSNPA
TNGMLRGDKP DLLHRAQSRA FVSGEGVPGP IEYFFASDAT PIIEYTKRVM FLEDDDIAHV
RDGELHVHRL RREGGGSTTR TIETLEMEIA SVMKGNYDHY MIKEICEQPD SLLNTMRGRV
NFVNRLVTLG GLESYYDIIR KSRRLIFVAC GTSYHSCVAV RPLFEELTNI PVVVELASDF
VDRCPSVFRD DTFIFVSQSG ETADSLLALQ YTLENGALAI GVVNCVGSSI SRKTHCGVHI
NAGPEICVAS TKAYTSQYVA LVLMALYLSR DSVSRLERRN EIIDGLAEIG EKVQETLHLN
AAIKQTAIEQ LINKDKMLII GRGYHYATAL EGALKVKEIS YTHAEGVLAG ELKHGVLALV
DNDMPIVMLL PDDYNFPKAW NAFEQVRARG GKPIIITDKK LDNLEGFTII KVPKTVDCLQ
GILNVIPFQL LSYWLAVKRG HNVDQPRNLA KSVTVE
