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Database: UniProt
Entry: B6IWN3_RHOCS
LinkDB: B6IWN3_RHOCS
Original site: B6IWN3_RHOCS 
ID   B6IWN3_RHOCS            Unreviewed;      1126 AA.
AC   B6IWN3;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   Name=glmS {ECO:0000313|EMBL:ACJ00707.1};
GN   OrderedLocusNames=RC1_3347 {ECO:0000313|EMBL:ACJ00707.1};
OS   Rhodospirillum centenum (strain ATCC 51521 / SW).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=414684 {ECO:0000313|EMBL:ACJ00707.1, ECO:0000313|Proteomes:UP000001591};
RN   [1] {ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA   Touchman J.W., Bauer C., Blankenship R.E.;
RT   "Genome sequence of Rhodospirillum centenum.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACJ00707.1, ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX   PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA   Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA   Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA   Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT   "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT   proteobacterium Rhodospirillum centenum.";
RL   BMC Genomics 11:325-325(2010).
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};
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DR   EMBL; CP000613; ACJ00707.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6IWN3; -.
DR   STRING; 414684.RC1_3347; -.
DR   KEGG; rce:RC1_3347; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_277828_0_0_5; -.
DR   OMA; NGDVDNY; -.
DR   Proteomes; UP000001591; Chromosome.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
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; 1.
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; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:ACJ00707.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001591};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACJ00707.1}.
FT   DOMAIN          2..423
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          503..653
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   1126 AA;  119591 MW;  882F37DE6D9E7042 CRC64;
     MCGIAGFLSN RHWTADPDLS WLDRAADALA AATPDDPAGI DAALDLLAGR FDALMSFGTH
     LAAATRPAVR ARLEAAAVRA QALEAALRAG PRAREEAVER VAERLRDYAW QLGTEVVANI
     DRTLALMPDA SAANRAQHLV AWGIGQTLEN LDRLEVRGRD SAGIAVLLRL APAAPLRDLR
     SLQAVAREAG REFGDQDGGI ALHALADGGL TARFTYKVAQ LIGRLGDNGA SLRARVRGDA
     LLWRLAAQAE GLSAIAHTRW ASHGAINLTN CHPLNGSLAG EAATELSADA DAVAVLNGDV
     DNYRALKETL VEAAGHAIAA PVTTDAKVIP VLFRLHQGNT PVEERVLATL RRLEGSMAIV
     VQHPDDPERL HLGQKGSGQS LFVAEGPDGL ILASENYGLA PRARASVALA QVERGGLAVV
     LSTRPGDPAL AARGIDDGAP AALKAEPIEI FSRDIFRGGF EHFFEKEVHE APASVRKTLA
     GRYRRGGREA AFETGEGSPW AALRRRLSDP DRPAVRRIWV TGQGTAAIAA MGVAHLIRQA
     LPGSGIQVES AKASELSADL EGAGLEDALV VAISQSGTTT DTNRTVDLAR AAGAWIHAIV
     NRRNSPLVRK SDSHLFTSDG RDIEMAVAST KAFYSQVAAG KLTALCLADA SGTLPPGQIH
     DELVCLESLP ARIQEVLDEE AEIARCAEAY APFNRYWAVV GNGPNKIAAE EIRIKLSELC
     YKSIPVDYTE DKKHIDLSTE PLTLVIANDM PAQLAQDTAK EVAIFKAHSG KPIVFCAKGE
     TCFDAYAEAV VRLPSAGAGL DFVLATVAGH LWGFHAARAI DARAHVFREL ASVVNERAAR
     DDARLDDVAD RLEAELERIA AGEMDAALPP RLAAGLALLA PKLRGFHQLP RCGAAEREAL
     AGRAEALLRA AFEETSRPID TIRHQAKTVT VGISRPGKEI GPVLLAALAA LEVAPTALAE
     HDRRMLAALS PLVTAVPGGI LYRQTGEGPD GAPLLQAARK CGRSAVPSGY DRPRPAAGSK
     RRALRLGRAI LSGGPHGRES LLLVPVFDEA DWEVTGLVLL HAELAPQASL QQKTALLKDL
     KLYEDLLDAF SETSHATGRT DFPAFVAAAS PRDLLFRPAA DLLRQP
//
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