ID AGAS_ECOLI Reviewed; 384 AA. AC P42907; Q2M974; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 152. DE RecName: Full=Putative D-galactosamine-6-phosphate deaminase AgaS {ECO:0000305}; DE EC=3.5.99.- {ECO:0000250|UniProtKB:Q9KIP9}; DE AltName: Full=Gam-6-P deaminase/isomerase {ECO:0000250|UniProtKB:Q9KIP9}; GN Name=agaS; Synonyms=yraB; OrderedLocusNames=b3136, JW3105; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [3] RP DISCUSSION OF SEQUENCE. RX PubMed=8932697; DOI=10.1099/13500872-142-2-231; RA Reizer J., Ramseier T.M., Reizer A., Charbit A., Saier M.H. Jr.; RT "Novel phosphotransferase genes revealed by bacterial genome sequencing: a RT gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in RT Escherichia coli."; RL Microbiology 142:231-250(1996). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RG Midwest center for structural genomics (MCSG); RT "The crystal structure of the tagatose-6-phosphate ketose/aldose isomerase RT from Escherichia coli."; RL Submitted (FEB-2008) to the PDB data bank. CC -!- FUNCTION: Catalyzes the isomerization-deamination of galactosamine 6- CC phosphate to form tagatofuranose 6-phosphate and ammonium ion. CC {ECO:0000250|UniProtKB:Q9KIP9}. 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:0000250|UniProtKB:Q9KIP9}; CC -!- MISCELLANEOUS: In contrast to E.coli strains C and EC3132, K-12 strains CC cannot grow on N-acetylgalactosamine and D-galactosamine, because they CC carry a deletion and thus lack active PTS systems specific for these CC compounds. Therefore, AgaS in K-12 strains is not involved in the CC degradation of these compounds. CC -!- SIMILARITY: Belongs to the SIS family. AgaS subfamily. {ECO:0000305}. 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; U18997; AAA57939.1; -; Genomic_DNA. DR EMBL; U00096; AAC76170.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77182.1; -; Genomic_DNA. DR PIR; D65103; D65103. DR RefSeq; NP_417605.1; NC_000913.3. DR RefSeq; WP_001114869.1; NZ_CP009789.1. DR PDB; 3C3J; X-ray; 1.80 A; A/B/C/D/E/F=1-384. DR AlphaFoldDB; P42907; -. DR SMR; P42907; -. DR BioGRID; 4261158; 784. DR FunCoup; P42907; 156. DR IntAct; P42907; 5. DR STRING; 511145.b3136; -. DR PaxDb; 511145-b3136; -. DR DNASU; 947645; -. DR EnsemblBacteria; AAC76170; AAC76170; b3136. DR GeneID; 947645; -. DR KEGG; ecj:JW3105; -. DR KEGG; eco:b3136; -. DR KEGG; ecoc:C3026_17090; -. DR PATRIC; fig|1411691.4.peg.3594; -. DR EchoBASE; EB2620; -. DR eggNOG; COG2222; Bacteria. DR HOGENOM; CLU_012520_0_0_6; -. DR InParanoid; P42907; -. DR OMA; KQQPELW; -. DR OrthoDB; 9779207at2; -. DR PhylomeDB; P42907; -. DR BioCyc; EcoCyc:G7634-MONOMER; -. DR EvolutionaryTrace; P42907; -. DR PRO; PR:P42907; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P42907; -. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro. DR GO; GO:0016853; F:isomerase activity; IEA:InterPro. DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central. DR CDD; cd05010; SIS_AgaS_like; 1. DR CDD; cd05008; SIS_GlmS_GlmD_1; 1. DR Gene3D; 3.40.50.10490; Glucose-6-phosphate isomerase like protein, domain 1; 2. DR InterPro; IPR050303; GatZ_KbaZ_carbometab. 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 NCBIfam; TIGR02815; agaS_fam; 1. DR PANTHER; PTHR32502:SF3; D-GALACTOSAMINE-6-PHOSPHATE DEAMINASE AGAS-RELATED; 1. DR PANTHER; PTHR32502; N-ACETYLGALACTOSAMINE PERMEASE II COMPONENT-RELATED; 1. DR Pfam; PF01380; SIS; 2. DR SUPFAM; SSF53697; SIS domain; 1. DR PROSITE; PS51464; SIS; 2. DR PDBsum; 3C3J; -. PE 1: Evidence at protein level; KW 3D-structure; Hydrolase; Reference proteome; Repeat. FT CHAIN 1..384 FT /note="Putative D-galactosamine-6-phosphate deaminase AgaS" FT /id="PRO_0000136590" 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" FT HELIX 6..9 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 15..21 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 23..49 FT /evidence="ECO:0007829|PDB:3C3J" FT STRAND 55..59 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 63..79 FT /evidence="ECO:0007829|PDB:3C3J" FT STRAND 81..85 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 88..93 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 95..98 FT /evidence="ECO:0007829|PDB:3C3J" FT STRAND 105..114 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 117..129 FT /evidence="ECO:0007829|PDB:3C3J" FT STRAND 131..140 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 145..151 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:3C3J" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 174..187 FT /evidence="ECO:0007829|PDB:3C3J" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:3C3J" FT TURN 194..197 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 198..210 FT /evidence="ECO:0007829|PDB:3C3J" FT TURN 211..213 FT /evidence="ECO:0007829|PDB:3C3J" FT STRAND 225..232 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 235..249 FT /evidence="ECO:0007829|PDB:3C3J" FT TURN 250..252 FT /evidence="ECO:0007829|PDB:3C3J" FT STRAND 253..259 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 261..264 FT /evidence="ECO:0007829|PDB:3C3J" FT TURN 265..267 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 268..271 FT /evidence="ECO:0007829|PDB:3C3J" FT STRAND 276..281 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 288..302 FT /evidence="ECO:0007829|PDB:3C3J" FT STRAND 305..314 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 317..320 FT /evidence="ECO:0007829|PDB:3C3J" FT STRAND 322..326 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:3C3J" FT HELIX 335..356 FT /evidence="ECO:0007829|PDB:3C3J" SQ SEQUENCE 384 AA; 41783 MW; 463F9458476DC46B CRC64; MPENYTPAAA ATGTWTEEEI RHQPRAWIRS LTNIDALRSA LNNFLEPLLR KENLRIILTG AGTSAFIGDI IAPWLASHTG KNFSAVPTTD LVTNPMDYLN PAHPLLLISF GRSGNSPESV AAVELANQFV PECYHLPITC NEAGALYQNA INSDNAFALL MPAETHDRGF AMTSSITTMM ASCLAVFAPE TINSQTFRDV ADRCQAILTS LGDFSEGVFG YAPWKRIVYL GSGGLQGAAR ESALKVLELT AGKLAAFYDS PTGFRHGPKS LVDDETLVVV FVSSHPYTRQ YDLDLLAELR RDNQAMRVIA IAAESSDIVA AGPHIILPPS RHFIDVEQAF CFLMYAQTFA LMQSLHMGNT PDTPSASGTV NRVVQGVIIH PWQA //