AGAI_ECOLI
ID AGAI_ECOLI Reviewed; 251 AA.
AC P42912; Q2M969;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Putative deaminase AgaI {ECO:0000305};
DE EC=3.5.99.- {ECO:0000305};
GN Name=agaI; Synonyms=yraG; OrderedLocusNames=b3141, JW3110;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 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 [3]
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 [4]
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 [5]
RP 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 -!- DISRUPTION PHENOTYPE: Deletion of the gene does not affect growth on N-
CC acetyl-D-galactosamine, D-galactosamine or N-acetyl-D-glucosamine.
CC {ECO:0000269|PubMed:23634833}.
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, AgaI in K-12 strains is not involved in the
CC degradation of these compounds.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be involved in the deamination and
CC isomerization of D-galactosamine 6-phosphate to D-tagatofuranose 6-
CC phosphate. {ECO:0000305|PubMed:23634833}.
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; AF228498; AAF81093.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57944.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76175.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77187.1; -; Genomic_DNA.
DR PIR; A65104; A65104.
DR RefSeq; NP_417610.1; NC_000913.3.
DR RefSeq; WP_001311150.1; NZ_LN832404.1.
DR AlphaFoldDB; P42912; -.
DR SMR; P42912; -.
DR BioGRID; 4261594; 5.
DR DIP; DIP-9069N; -.
DR IntAct; P42912; 4.
DR STRING; 511145.b3141; -.
DR PaxDb; P42912; -.
DR PRIDE; P42912; -.
DR EnsemblBacteria; AAC76175; AAC76175; b3141.
DR EnsemblBacteria; BAE77187; BAE77187; BAE77187.
DR GeneID; 947985; -.
DR KEGG; ecj:JW3110; -.
DR KEGG; eco:b3141; -.
DR PATRIC; fig|511145.12.peg.3236; -.
DR EchoBASE; EB2625; -.
DR eggNOG; COG0363; Bacteria.
DR HOGENOM; CLU_049611_1_1_6; -.
DR InParanoid; P42912; -.
DR OMA; FSNTQFV; -.
DR PhylomeDB; P42912; -.
DR BioCyc; EcoCyc:G7636-MON; -.
DR PRO; PR:P42912; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043877; F:galactosamine-6-phosphate isomerase activity; NAS:EcoliWiki.
DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006043; P:glucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
DR CDD; cd01399; GlcN6P_deaminase; 1.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR004547; Glucosamine6P_isomerase.
DR InterPro; IPR018321; Glucosamine6P_isomerase_CS.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR11280; PTHR11280; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..251
FT /note="Putative deaminase AgaI"
FT /id="PRO_0000160189"
FT ACT_SITE 86
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000250"
FT ACT_SITE 154
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000250"
FT ACT_SITE 161
FT /note="For ring-opening step"
FT /evidence="ECO:0000250"
SQ SEQUENCE 251 AA; 27724 MW; 823CB4CFBD82B8C6 CRC64;
MERGTASGGA SLLKEFHPVQ TLQQVENYTA LSERASEYLL AVIRSKPNAV ICLATGATPL
LTYHYLVEKI HQQQVDVSQL TFVKLDEWVD LPLTMPGTCE TFLQQHIVQP LGLREDQLIS
FRSEEINETE CERVTNLIAR KGGLDLCVLG LGKNGHLGLN EPGESLQPAC HISQLDARTQ
QHEMLKTAGR PVTRGITLGL KDILNAREVL LLVTGEGKQD ATDRFLTAKV STAIPASFLW
LHSNFICLIN T