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Database: UniProt
Entry: S2JJU6_MUCC1
LinkDB: S2JJU6_MUCC1
Original site: S2JJU6_MUCC1 
ID   S2JJU6_MUCC1            Unreviewed;       687 AA.
AC   S2JJU6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|ARBA:ARBA00033302};
DE   AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|ARBA:ARBA00029805};
GN   ORFNames=HMPREF1544_04407 {ECO:0000313|EMBL:EPB88767.1};
OS   Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS   agent) (Calyptromyces circinelloides).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB88767.1, ECO:0000313|Proteomes:UP000014254};
RN   [1] {ECO:0000313|Proteomes:UP000014254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in amino sugar synthesis (formation of chitin,
CC       supplies the amino sugars of asparagine-linked oligosaccharides of
CC       glycoproteins). {ECO:0000256|ARBA:ARBA00003267}.
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   -!- 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. {ECO:0000256|ARBA:ARBA00004775}.
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DR   EMBL; KE123945; EPB88767.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2JJU6; -.
DR   STRING; 1220926.S2JJU6; -.
DR   VEuPathDB; FungiDB:HMPREF1544_04407; -.
DR   eggNOG; KOG1268; Eukaryota.
DR   InParanoid; S2JJU6; -.
DR   OrthoDB; 1705390at2759; -.
DR   UniPathway; UPA00113; UER00528.
DR   Proteomes; UP000014254; 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:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
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:EPB88767.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014254};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPB88767.1}.
FT   DOMAIN          2..291
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          365..504
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          537..677
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   687 AA;  76330 MW;  023497E0EEF75225 CRC64;
     MCGIFGYCNF LCEKSRREVC DTLLNGLSRL EYRGYDSAGF AVDGDNDDIL IMKQVGKVAA
     LRKLVDEQQL DFSKPCISQC GMAHTRWATH GQPSQINSHP QRSDEKNEFA LVHNGIITNY
     KEIKLLLEKK GYVFESDTDT ECVAKLTKYV YDSHNKDMSF TELVKAVVKE LEGSYAFIFK
     STHFPNEIVA TRRGSPLLIG VKTAKKLKVD FVDVEFGGNN AAGTDSSFAP VEGQDMSRPA
     LNRSQSRAFL SEDGMPQPIE YFLASDASAI VEHTKRVLYL EDDDIAHIAD GELHIHRVRR
     SKEDNTPATR SIQTLEIELA EIMKGSFDHF MQKEIYEQPE SVVNTMRGRV NFENHEVTLG
     GLRGFTHIIR RARRIIFIAC GTSYHSCLAT RSIFEELNQI GTQAELASDF LDRASPIFRD
     DVCVFVSQSG ETADTILAMR YCLERGALCV GVTNTVGSSI SRETHCGVHI NAGPEIGVAS
     TKAYTSQYIA LVMMALQLAE DTTSTKQRRE EIIDGLYRLP GHIKEVLAID GKLQQLAVDQ
     LAHEKSLLIL GRGYQNATCL EGALKIKEIS YIHSEGILAG ELKHGPLALI DEHMPVILLM
     TQDSLYPKVQ SALQQVAARK GTPIIICNTG DQNLVNSYKT IEVPKTSDCL QGLINIIPLQ
     LLSYHLAILK GVDVDFPRNL AKSVTVE
//
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