(data stored in SCRATCH zone)

SWISSPROT: A1AZN7_PARDP

ID   A1AZN7_PARDP            Unreviewed;       605 AA.
AC   A1AZN7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 99.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164, ECO:0000256|SAAS:SAAS00887593};
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=Pden_0619 {ECO:0000313|EMBL:ABL68731.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68731.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism,
CC       converting fructose-6P into glucosamine-6P using glutamine as a
CC       nitrogen source. {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,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725,
CC         ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={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       ECO:0000256|SAAS:SAAS00887591}.
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DR   EMBL; CP000489; ABL68731.1; -; Genomic_DNA.
DR   RefSeq; WP_011746964.1; NC_008686.1.
DR   STRING; 318586.Pden_0619; -.
DR   PRIDE; A1AZN7; -.
DR   EnsemblBacteria; ABL68731; ABL68731; Pden_0619.
DR   KEGG; pde:Pden_0619; -.
DR   eggNOG; ENOG4105C46; Bacteria.
DR   eggNOG; COG0449; LUCA.
DR   HOGENOM; HOG000258896; -.
DR   KO; K00820; -.
DR   OMA; ASEYRYA; -.
DR   BioCyc; PDEN318586:G1GW1-626-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; A1AZN7.
DR   SWISS-2DPAGE; A1AZN7.
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000313|EMBL:ABL68731.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000256|SAAS:SAAS00887588};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000313|EMBL:ABL68731.1}.
FT   INIT_MET      1      1       Removed. {ECO:0000256|HAMAP-Rule:
FT                                MF_00164}.
FT   DOMAIN        2    218       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   DOMAIN      281    420       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   DOMAIN      453    595       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   ACT_SITE      2      2       Nucleophile; for GATase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00164}.
FT   ACT_SITE    600    600       For Fru-6P isomerization activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00164}.
SQ   SEQUENCE   605 AA;  64943 MW;  78D22FECFA1261E3 CRC64;
     MCGIIGILGD HEVSPQLVEA LKRLEYRGYD SAGVATVDAS GHLDRRRAVG KLVNLSDRLV
     HEPLAGHAGI GHTRWATHGA ATEANAHPHR RGPVAVVHNG IIENFRELRD EVTRLGMQPE
     SQTDTETVAL LTAWHMGQGL APVEAARAVL ARLDGAFALA FLFEGEPDLM IAARKGSPLA
     VGHGEGEMFL GSDAIALAPF TDRITYLEDG DHAVIRRSGA EIFDAEGRPA NREIQQIDVG
     ATRIDKGGYR HFMAKEIAEQ PVVLGDALNH YIKGDRIVLP EALDFRDVDR LTLVGCGTAF
     YAAHVARYWF ESLAGLPCDL DVASEFRYRE PPLSPASWAI FVSQSGETAD TLAALHYARD
     KVARTVGVVN VGTSAIARDA DIALPTLAGI EVGVASSKAF TCQLAVLAVL ALKAARDRGR
     LTDSELAAHL ADLRALPGLL NQALTVSDEC RRLAGWLAEA QDVLYLGRGA LYPVALEGAL
     KLKELSYIHA EGYASGELKH GPIALIDRNV PVVVLAPRDA LFEKTVSNMQ EVMARHGQVL
     LISDPEGLET GGHGIHARLA MPPGGGLFQP ILYAVPMQYL AYHTAVAKGT DVDQPRNLAK
     SVTVE
//

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