(data stored in ACNUC13767 zone)

SWISSPROT: Q2YCA0_NITMU

ID   Q2YCA0_NITMU            Unreviewed;       615 AA.
AC   Q2YCA0;
DT   20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2005, sequence version 1.
DT   11-DEC-2019, entry version 108.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164, ECO:0000256|SAAS:SAAS01229024};
DE            EC=2.6.1.16 {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   OrderedLocusNames=Nmul_A0313 {ECO:0000313|EMBL:ABB73621.1};
GN   ORFNames=SAMN05216403_10133 {ECO:0000313|EMBL:SEF39030.1};
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848 {ECO:0000313|EMBL:ABB73621.1, ECO:0000313|Proteomes:UP000002718};
RN   [1] {ECO:0000313|Proteomes:UP000002718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71
RC   {ECO:0000313|Proteomes:UP000002718};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABB73621.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB73621.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of Chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ABB73621.1, ECO:0000313|Proteomes:UP000002718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB73621.1}, and ATCC 25196 /
RC   NCIMB 11849 / C 71 {ECO:0000313|Proteomes:UP000002718};
RX   PubMed=18390676; DOI=10.1128/AEM.02722-07;
RA   Norton J.M., Klotz M.G., Stein L.Y., Arp D.J., Bottomley P.J., Chain P.S.,
RA   Hauser L.J., Land M.L., Larimer F.W., Shin M.W., Starkenburg S.R.;
RT   "Complete genome sequence of Nitrosospira multiformis, an ammonia-oxidizing
RT   bacterium from the soil environment.";
RL   Appl. Environ. Microbiol. 74:3559-3572(2008).
RN   [4] {ECO:0000313|EMBL:SEF39030.1, ECO:0000313|Proteomes:UP000236751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nl13 {ECO:0000313|EMBL:SEF39030.1,
RC   ECO:0000313|Proteomes:UP000236751};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|HAMAP-Rule:MF_00164};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164,
CC       ECO:0000256|SAAS:SAAS01229031}.
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DR   EMBL; CP000103; ABB73621.1; -; Genomic_DNA.
DR   EMBL; FNVK01000001; SEF39030.1; -; Genomic_DNA.
DR   RefSeq; WP_011379675.1; NZ_FNVK01000001.1.
DR   STRING; 323848.Nmul_A0313; -.
DR   EnsemblBacteria; ABB73621; ABB73621; Nmul_A0313.
DR   GeneID; 41369136; -.
DR   KEGG; nmu:Nmul_A0313; -.
DR   eggNOG; ENOG4105C46; Bacteria.
DR   eggNOG; COG0449; LUCA.
DR   HOGENOM; HOG000258898; -.
DR   KO; K00820; -.
DR   OMA; TSYYSGC; -.
DR   OrthoDB; 43416at2; -.
DR   BioCyc; NMUL323848:G1GTI-328-MONOMER; -.
DR   Proteomes; UP000002718; Chromosome.
DR   Proteomes; UP000236751; 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   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 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.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q2YCA0.
DR   SWISS-2DPAGE; Q2YCA0.
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000313|EMBL:ABB73621.1};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164, ECO:0000256|SAAS:SAAS01229030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002718};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00164, ECO:0000313|EMBL:ABB73621.1}.
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          291..431
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          464..605
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        610
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   615 AA;  67250 MW;  21389A8DAE36E209 CRC64;
     MCGIVGAVAK TNIVPTLIEG LRRLEYRGYD SAGIALNNGR LHRLRTTGRV AELSKLADEQ
     HFTGDVGIAH TRWATHGAPS ERNAHPHFSG ETPKVAVVHN GIIENHEVLR QRLQKTGFEF
     SSETDTEVIA HLISSHLREN PDLFEAVCRS VGELRGAYAI AVMEEARPER LIVCRNGAPL
     LLGLGENGIY AASDASALLQ VTRRMIYLEE GDVAELRQDG YRIVNCRYDG ARAEVARAVQ
     ESELTNEAVE MGPYAHFMQK EIFEQPGVVA NTLEMVLNAQ SISPRLFGTE AENIFKNTRS
     ILILACGTSY HAGVVARYWL ETVAGIPCNV EIASEYRYRN PAVGADTLIV GISQSGETAD
     TLAALSYAKS LGHRYSLGIC NVAESALVRQ TDLRFLTRAG PEIGVASTKA FTTQLAALML
     LTMTLAKLNG KLSGESERQM IAALRHLPVA LQHSLQVEPQ VKAWAERFAE KRHALFLGRG
     MHYPIALEGA LKLKEISYIH AEAYAAGELK HGPLALVDKD MPVVAIAPND ALLEKLKSNL
     QEVRARGGEL YVFADADSHI QESEGVHIIR LAEHAGMLSP ILHTIPLQLL AYHVALQKGT
     DVDKPRNLAK SVTVE
//

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