AGAS_ECOLI
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 03-AUG-2022, entry version 136.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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}.
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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_LN832404.1.
DR PDB; 3C3J; X-ray; 1.80 A; A/B/C/D/E/F=1-384.
DR PDBsum; 3C3J; -.
DR AlphaFoldDB; P42907; -.
DR SMR; P42907; -.
DR BioGRID; 4261158; 779.
DR IntAct; P42907; 5.
DR STRING; 511145.b3136; -.
DR PaxDb; P42907; -.
DR PRIDE; P42907; -.
DR DNASU; 947645; -.
DR EnsemblBacteria; AAC76170; AAC76170; b3136.
DR EnsemblBacteria; BAE77182; BAE77182; BAE77182.
DR GeneID; 66672963; -.
DR GeneID; 947645; -.
DR KEGG; ecj:JW3105; -.
DR KEGG; eco:b3136; -.
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; YHLIITC; -.
DR PhylomeDB; P42907; -.
DR BioCyc; EcoCyc:G7634-MON; -.
DR EvolutionaryTrace; P42907; -.
DR PRO; PR:P42907; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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 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 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 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 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
