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Database: UniProt
Entry: Q0EZN3_9PROT
LinkDB: Q0EZN3_9PROT
Original site: Q0EZN3_9PROT 
ID   Q0EZN3_9PROT            Unreviewed;       608 AA.
AC   Q0EZN3;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090, ECO:0000256|HAMAP-Rule:MF_00164};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916, ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=GFAT {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
GN   Name=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN   ORFNames=SPV1_13844 {ECO:0000313|EMBL:EAU54671.1};
OS   Mariprofundus ferrooxydans PV-1.
OC   Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC   Mariprofundaceae; Mariprofundus.
OX   NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU54671.1, ECO:0000313|Proteomes:UP000005297};
RN   [1] {ECO:0000313|EMBL:EAU54671.1, ECO:0000313|Proteomes:UP000005297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV-1 {ECO:0000313|EMBL:EAU54671.1,
RC   ECO:0000313|Proteomes:UP000005297};
RA   Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC       fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC       {ECO:0000256|HAMAP-Rule:MF_00164}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00164};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164}.
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:EAU54671.1}.
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DR   EMBL; AATS01000006; EAU54671.1; -; Genomic_DNA.
DR   RefSeq; WP_009850281.1; NZ_DS022294.1.
DR   AlphaFoldDB; Q0EZN3; -.
DR   STRING; 314344.AL013_10260; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_5_2_0; -.
DR   InParanoid; Q0EZN3; -.
DR   OrthoDB; 5287359at2; -.
DR   Proteomes; UP000005297; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00164; GlmS; 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   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW   Rule:MF_00164}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005297};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00164}.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT   DOMAIN          2..219
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          287..426
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          458..598
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT   ACT_SITE        603
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   608 AA;  65865 MW;  CDBAD84B210F38AD CRC64;
     MCGIVGAIAG RNVLPILMDG LQRLEYRGYD SAGVAIRDAA GELLRFRALG KVSVLKELVD
     RSDIAGDLGI AHTRWATHGA PSERNAHPHM SGVRVAVVHN GIIENHRELR DRLLALGYTF
     TSETDTEVIA HLLAHKLEGG RDLYAAVVEA AAELDGAYAL AAASPEDPDR IVVTREGSPL
     VIGLGEGENF IASDVAALLP VTRRFIFLEE GDVAEVRRDG VTVCDGDGIE VVREIKTSEL
     SSASIDKGLY AHYMLKEIYE QPAVIAETLE GRIHKGRLLE ASFGHETTAL LDKARHIQIV
     ACGTSYHAGM VARYWMEEFG IPCSVEVASE YRYRKVVVPE GSLLITISQS GETADTLAAL
     RGSRANGYIG SLTVCNVPES SLVRESDVCF MTRAGTEIGV ASTKAFTTQL VALRLLAIAL
     ARRKELSTAQ EEAMVNELHA LPRQIEVVLQ LADAIKTMAE GFVDKHNALF LGRGAFYPVA
     LEGALKLKEI SYIHAEAYPA GELKHGPLAL VDESMPVVCA LPDDPLLEKV LSNLQEVRAR
     GGELFLFSDH KVNVGLDHYQ NLTLSDIYPG TAPIVYSIPL QLLAYHVAVL KGTDVDQPRN
     LAKSVTVE
//
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