ID A0A077HGP8_9CORY Unreviewed; 621 AA.
AC A0A077HGP8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=CUREI_01625 {ECO:0000313|EMBL:AIL96183.1};
OS Corynebacterium ureicelerivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=401472 {ECO:0000313|EMBL:AIL96183.1, ECO:0000313|Proteomes:UP000028939};
RN [1] {ECO:0000313|EMBL:AIL96183.1, ECO:0000313|Proteomes:UP000028939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMMIB RIV-2301 {ECO:0000313|EMBL:AIL96183.1,
RC ECO:0000313|Proteomes:UP000028939};
RA Tippelt A., Albersmeier A., Brinkrolf K., Ruckert C., Tauch A.;
RT "Complete genome sequence of Corynebacterium ureicelerivorans DSM 45051, a
RT lipophilic and urea-splitting isolate from a blood culture of a septicaemia
RT patient.";
RL Submitted (AUG-2014) 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}.
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DR EMBL; CP009215; AIL96183.1; -; Genomic_DNA.
DR RefSeq; WP_038609649.1; NZ_CP009215.1.
DR AlphaFoldDB; A0A077HGP8; -.
DR STRING; 401472.CUREI_01625; -.
DR KEGG; cuv:CUREI_01625; -.
DR HOGENOM; CLU_012520_5_2_11; -.
DR OrthoDB; 9761808at2; -.
DR Proteomes; UP000028939; Chromosome.
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 ECO:0000313|EMBL:AIL96183.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028939};
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..226
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 293..433
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 466..611
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 616
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 621 AA; 67255 MW; ED8AE0E3FD093842 CRC64;
MCGIVGYVSA GAAERDAENV IIEGLRRLEY RGYDSAGVAV ANNGVIECRK KAGKVADLEA
LIADNPIPSS NLGIGHTRWA THGGPTDVNA HPHVVGGGRL AVVHNGIIEN FAGLKAELVD
KGYTFASETD TEVAGMLLLD IYDKEAEGDL TRAMQLTAQR LEGAFTLLAI HADHPDRIVA
ARWNSPLVIG VGEGENFLGS DVAGFIEFTR DAVEMDNGQI VTLTADGYEV CDFEGNPAQG
KPFTVEWDVT AAEKGGYNSF MEKEIHDQPA AVRDTLYGRF DEEGKLTLDE LRIDESLLRS
INKIIIVACG TASYAGQVAR YAIEHWCRIP TEVELAHEFR YRDPIVNEHT LVVAVSQSGE
TMDTLMAVRH AREQGAKVIA ICNTVGSSIP READASLYTY AGPEIAVAST KAFISQIVAA
YLLALYLAQV RGNKYADEIR QIVDELQQMP DKIQRVLDNE GQVKQLGQEM ADAKSVLFLG
RHVGFPVALE GALKLKEVAY LHSEGFAAGE LKHGPIALVE EGQPVFIIVP SKRSRNNLHA
KVVSNIQEVR ARGAVTIVIA EEGDTDVEAY ADHIIRIPES AGLMQPLLST IPLQIFACAV
AEARGLNVDQ PRNLAKSVTV E
//
