ID   AGAS_ECO57              Reviewed;         384 AA.
AC   Q8XAC2; Q7AAK2;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 125.
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};
GN   OrderedLocusNames=ECs4016 {ECO:0000312|EMBL:BAB37439.1},
GN   Z4490 {ECO:0000312|EMBL:AAG58268.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
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. {ECO:0000269|PubMed:23634833}.
CC   -!- SIMILARITY: Belongs to the SIS family. AgaS subfamily. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58268.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37439.1; -; Genomic_DNA.
DR   PIR; H85975; H85975.
DR   PIR; H91130; H91130.
DR   RefSeq; NP_312043.1; NC_002695.1.
DR   RefSeq; WP_001114858.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XAC2; -.
DR   SMR; Q8XAC2; -.
DR   STRING; 155864.EDL933_4359; -.
DR   EnsemblBacteria; AAG58268; AAG58268; Z4490.
DR   EnsemblBacteria; BAB37439; BAB37439; ECs_4016.
DR   GeneID; 916150; -.
DR   KEGG; ece:Z4490; -.
DR   KEGG; ecs:ECs_4016; -.
DR   PATRIC; fig|386585.9.peg.4192; -.
DR   eggNOG; COG2222; Bacteria.
DR   HOGENOM; CLU_012520_0_0_6; -.
DR   OMA; YHLIITC; -.
DR   BioCyc; MetaCyc:MON-18272; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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; Reference proteome; Repeat.
FT   CHAIN           1..384
FT                   /note="D-galactosamine-6-phosphate deaminase AgaS"
FT                   /id="PRO_0000441911"
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;  41729 MW;  3D07F99238BE062B CRC64;
     MPENYTPAAA ATGTWTEEEI RHQPRAWIRS LTNIDALHSA LNNFLEPLLR KENLRIILTG
     AGTSAFIGDI IAPWLASHTG KNFSAVPTTD LVTNPMDYLN PAHPLLLISF GRSGNSPESV
     AAVELANQFV PECYHLPITC NEAGALYQNA INSDNAFAVL MPAETHDRGF AMTSSITTMM
     ASCLAVFAPE TINSQTFRDV ADRCQAILTS LGDFSEGVFG YAPWKRIVYL GSGGLQGAAR
     ESALKVLELT AGKLAAFYDS PTGFRHGPKS LVDNETLVVV FVSSHPYTRQ YDLDLLAELH
     RDNQAMRVIA IAAESSDIVA AGPHIILPPS RHFIDVEQAF CFLMYAQTFA LMQSLHMGNT
     PDTPSASGTV NRVVQGVIIH PWQA