AGAS_ECOLX
ID AGAS_ECOLX Reviewed; 384 AA.
AC Q9KIP9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=D-galactosamine-6-phosphate deaminase AgaS {ECO:0000305};
DE EC=3.5.99.- {ECO:0000305|PubMed:23634833};
DE AltName: Full=Gam-6-P deaminase/isomerase {ECO:0000303|PubMed:23634833};
GN Name=agaS {ECO:0000303|PubMed:23634833};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PUTATIVE FUNCTION.
RC STRAIN=C;
RX PubMed=10931310; DOI=10.1046/j.1365-2958.2000.01969.x;
RA Brinkkoetter A., Kloess H., Alpert C.-A., Lengeler J.W.;
RT "Pathways for the utilization of N-acetyl-galactosamine and galactosamine
RT in Escherichia coli.";
RL Mol. Microbiol. 37:125-135(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=C;
RX PubMed=23634833; DOI=10.1186/1471-2180-13-94;
RA Hu Z., Patel I.R., Mukherjee A.;
RT "Genetic analysis of the roles of agaA, agaI, and agaS genes in the N-
RT acetyl-D-galactosamine and D-galactosamine catabolic pathways in
RT Escherichia coli strains O157:H7 and C.";
RL BMC Microbiol. 13:94-94(2013).
CC -!- FUNCTION: Catalyzes the isomerization-deamination of galactosamine 6-
CC phosphate to form tagatofuranose 6-phosphate and ammonium ion.
CC {ECO:0000305|PubMed:23634833}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactosamine 6-phosphate + H2O = D-tagatopyranose 1-
CC phosphate + NH4(+); Xref=Rhea:RHEA:47680, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:71674, ChEBI:CHEBI:138150;
CC Evidence={ECO:0000305|PubMed:23634833};
CC -!- INDUCTION: Induced by growth on N-acetyl-D-galactosamine.
CC {ECO:0000269|PubMed:23634833}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant does not grow on N-acetyl-D-
CC galactosamine or D-galactosamine. {ECO:0000269|PubMed:23634833}.
CC -!- SIMILARITY: Belongs to the SIS family. AgaS subfamily. {ECO:0000305}.
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DR EMBL; AF228498; AAF81088.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KIP9; -.
DR SMR; Q9KIP9; -.
DR STRING; 585034.ECIAI1_3286; -.
DR eggNOG; COG2222; Bacteria.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:InterPro.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd05010; SIS_AgaS_like; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035464; SIS_AgaS.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR014180; Sugar_isomerase_AgaS.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR02815; agaS_fam; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Hydrolase; Repeat.
FT CHAIN 1..384
FT /note="D-galactosamine-6-phosphate deaminase AgaS"
FT /id="PRO_0000355317"
FT DOMAIN 45..197
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 215..364
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
SQ SEQUENCE 384 AA; 41797 MW; 946DC35D123DC788 CRC64;
MPENYTPAAA ATGTWTEEEI RHQPRAWIRS LTNIDALRSA LNNFLEPLLR KENLRIILTG
AGTSAFIGDI IAPWLASHTG KNFSAVPTTD LVTNPMDYLN PAHPLLLISF GRSGNSPESV
AAVELANQFV PECYHLPITC NEAGALYQNA INSDNAFALL MPAETHDRGF AMTSSITTMM
ASCLAVFAPE TINSQTFRDV ADRCQAILTT LGDFSEGVFG YAPWKRIVYL GSGGLQGAAR
ESALKVLELT AGKLAAFYDS PTGFRHGPKS LVDDETLVVV FVSSHPYTRQ YDLDLLAELR
RDNQAMRVIA IAAESSDIVA AGPHIILPPS RHFIDVEQAF CFLMYAQTFA LMQSLHMGNT
PDTPSASGTV NRVVQGVIIH PWQA
