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GLMS_BRADU
ID   GLMS_BRADU              Reviewed;         608 AA.
AC   P59362;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE            EC=2.6.1.16;
DE   AltName: Full=D-fructose-6-phosphate amidotransferase;
DE   AltName: Full=GFAT;
DE   AltName: Full=Glucosamine-6-phosphate synthase;
DE   AltName: Full=Hexosephosphate aminotransferase;
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase;
GN   Name=glmS; OrderedLocusNames=bll4607;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC       fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC       {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; BA000040; BAC49872.1; -; Genomic_DNA.
DR   RefSeq; NP_771247.1; NC_004463.1.
DR   RefSeq; WP_011087378.1; NZ_CP011360.1.
DR   AlphaFoldDB; P59362; -.
DR   SMR; P59362; -.
DR   STRING; 224911.27352871; -.
DR   PRIDE; P59362; -.
DR   EnsemblBacteria; BAC49872; BAC49872; BAC49872.
DR   GeneID; 64024360; -.
DR   KEGG; bja:bll4607; -.
DR   PATRIC; fig|224911.44.peg.4408; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_5_2_5; -.
DR   InParanoid; P59362; -.
DR   OMA; ASEYRYA; -.
DR   PhylomeDB; P59362; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
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_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF53697; SSF53697; 1.
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;
KW   Aminotransferase; Cytoplasm; Glutamine amidotransferase;
KW   Reference proteome; Repeat; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..608
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000135307"
FT   DOMAIN          2..217
FT                   /note="Glutamine amidotransferase type-2"
FT   DOMAIN          284..423
FT                   /note="SIS 1"
FT   DOMAIN          456..598
FT                   /note="SIS 2"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        603
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   608 AA;  66370 MW;  A2627F79781AF783 CRC64;
     MCGIVGILGR EPVAEQLVDS LKRLEYRGYD SAGVATLEGR HLERRRAEGK LKNLEKRLEA
     EPLKGTTGIG HTRWATHGKP TVNNAHPHAT ERVAVVHNGI IENFRELREE LEKNGTVFHT
     ETDTEIVLHL VDDLLTRGNK PVEAVKLALA RLRGAFALGF IFAGDNDLMI GARNGPPLAI
     GYGDGEMYLG SDAIALGPFT DTISYLEDGD WVVLTRNSAT IFDKDGHAVQ REKIKHAAST
     SLVDKANYRH FMAKEIHEQP EVVGHTLARY VDMATERVSL PVKLPFDFKN IQRINITACG
     TASYAGFVAK YWFERFARLP VEVDVASEFR YREAPLRKGD LAIFISQSGE TADTLAALRY
     AKAEGVHTVA VVNVPTSTIA RESETVLPTL AGPEIGVAST KAFTCQLMVL ANLAIAAGKA
     RGELSDEDET KLVHGLVEIP RLMSDALTTE LQIEKLAREI AKSRDVLYLG RGTSFPLALE
     GALKLKEISY IHAEGYAAGE LKHGPIALID ETMPVVVIAP YDRVFEKTVS NMQEVAARGG
     KIILMTDAKG AEEATVESLV TIVMPDMAAA FTPMVYAVPV QLLAYHTAVI MGTDVDQPRN
     LAKSVTVE
 
 
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