(data stored in SCRATCH zone)

SWISSPROT: D6ZB79_SEGRD

ID   D6ZB79_SEGRD            Unreviewed;       616 AA.
AC   D6ZB79;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
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=Srot_0351 {ECO:0000313|EMBL:ADG96838.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96838.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96838.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001958; ADG96838.1; -; Genomic_DNA.
DR   RefSeq; WP_013137294.1; NC_014168.1.
DR   STRING; 640132.Srot_0351; -.
DR   EnsemblBacteria; ADG96838; ADG96838; Srot_0351.
DR   KEGG; srt:Srot_0351; -.
DR   eggNOG; ENOG4105C46; Bacteria.
DR   eggNOG; COG0449; LUCA.
DR   HOGENOM; HOG000258896; -.
DR   KO; K00820; -.
DR   OMA; ASEYRYA; -.
DR   OrthoDB; 43416at2; -.
DR   BioCyc; SROT640132:G1GLH-352-MONOMER; -.
DR   Proteomes; UP000002247; 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   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; D6ZB79.
DR   SWISS-2DPAGE; D6ZB79.
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000313|EMBL:ADG96838.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000256|SAAS:SAAS00887588};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000313|EMBL:ADG96838.1}.
FT   INIT_MET      1      1       Removed. {ECO:0000256|HAMAP-Rule:
FT                                MF_00164}.
FT   DOMAIN        2    224       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   DOMAIN      291    430       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   DOMAIN      463    606       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   ACT_SITE      2      2       Nucleophile; for GATase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00164}.
FT   ACT_SITE    611    611       For Fru-6P isomerization activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00164}.
SQ   SEQUENCE   616 AA;  66271 MW;  385536E40C23D329 CRC64;
     MCGIIGYVGH RQASPVLMEA LRRMEYRGYD SAGVAVVADD RTLATAKKAG RIANLERVLA
     AMPQVPGQLG MGHTRWATHG RPTDRNAHPH LDPAGQVAVV HNGIIENHLR LRMELEAEGV
     EFASDTDSEV AVHLVARAVA DGPTKGDFVA SVRSVVQRLH GAFTLVFAHA EHPGTIVAAR
     RSTPLILGVG QGEMFLASDV AAFIEHTREA VELGQDEVVA ITCDGYQIWS FGGEQRTGKP
     FHIDWDLAAA EKSGYEHFML KEIAEQPQAI ADTLLGHFDG GRVVLDEQRF TDQDLRDVDK
     IFVVACGSAH LSGLIAKYAI EHWTRLPVEV ELASEFRYRD PVLDSSTLVL AISQSGETLD
     TLEAVRHAKE QGAKVLAICN TNGAQIPREA DGVLYTHAGP EIAVASTKGF ITQVVANYLV
     GLALAGARGT KYPDEVAREI AELEAIPDLL RHVLGQMEPV RELATQLSGA STILFLGRHM
     GYPVALEGAL KLKELAYMHA EGFAAGELKH GPIALVEEGV PIVVVAPPVK SMLHAKVLSN
     IQEVQARGAR TIVIAEEGDD AAAPHADHLF TVPAVSTLWQ PLLAVVPLQV FAAQVAIARG
     LDVDKPRNLA KSVTVE
//

If you have problems or comments...

PBIL Back to PBIL home page