ID L5JVV4_PTEAL Unreviewed; 708 AA.
AC L5JVV4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=PAL_GLEAN10016986 {ECO:0000313|EMBL:ELK03192.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK03192.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB031114; ELK03192.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JVV4; -.
DR STRING; 9402.L5JVV4; -.
DR eggNOG; KOG1268; Eukaryota.
DR InParanoid; L5JVV4; -.
DR UniPathway; UPA00113; UER00528.
DR Proteomes; UP000010552; 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:SF10; GLUTAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE [ISOMERIZING] 2; 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:0000313|EMBL:ELK03192.1};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELK03192.1}.
FT DOMAIN 26..312
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 386..525
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 557..698
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 708 AA; 79827 MW; 6523754E8AB0410E CRC64;
MPMCPDCVLR TTNPVFYKAL CHPLLTGIFA YMNYRVPRTR KEIFETLIKG LQRLEYRGYD
SAGVAIDGNN NEVKERHIQL VKKRGNVKAL DEELYKQDSM DLEVEFETHF GIAHTRWATH
GVPSVVNSHP QRSDKGNEFV VIHNGIITNY KDLRKFLESK GYEFESETDT ETIAKLIKYV
FDNREIEDIT FSTLVERVIQ QLEGAFALVF KSIHYPGEAV ATRRGSPLLI GVRSEHKLST
EQIPILYRTR SIENAKNICK SRTKRLDSST CLHAVGDKAV EFFFASDASA IIEHTNRVIF
LEDDDIAAVA DGKLSIHRVK RSASDDPSRA IQTLQMELQQ IMKGRCNFSA FMQKEIFEQP
ESVFNTMRGR VNFETSTVLL GGLKAHLKEI RRCRRLIVIG CGTSYHAALA TRQVLEELTE
LPVMVELASD FLDRNTPVFR DDVCFFISQS GETADTLLAL RYCKDRGALT VGVTNTVGSS
ISRETDCGVH INAGPEIGVA STKAYTSQFI SLVMFGLMMS EDRISLQDRR REIILGLQSL
PELIKEVLSL DEKIHDLALE LYMQRSLLVM GRGYNYATCL EGALKIKEIT YMHSEGILAG
ELKHGPLALI DKQMPIIMII MKDPCFAKCQ NALQQITARQ GRPIILCSKD DTESSKFAYK
MIELPPTVDC LQGVLSVIPL QLLSFHLAVL RGYDVDFPRN LAKSVTVE
//
