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   04-NOV-2026, entry version 151.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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_CP010445.1.
DR   AlphaFoldDB; P42912; -.
DR   SMR; P42912; -.
DR   BioGRID; 4261594; 9.
DR   DIP; DIP-9069N; -.
DR   FunCoup; P42912; 130.
DR   IntAct; P42912; 4.
DR   STRING; 511145.b3141; -.
DR   PaxDb; 511145-b3141; -.
DR   EnsemblBacteria; AAC76175; AAC76175; b3141.
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; ADEQECA; -.
DR   OrthoDB; 9810967at2; -.
DR   PhylomeDB; P42912; -.
DR   BioCyc; EcoCyc:G7636-MONOMER; -.
DR   PRO; PR:P42912; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P42912; -.
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:D-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   Gene3D; 3.40.50.1360; -; 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   NCBIfam; NF007291; PRK09762.1; 1.
DR   PANTHER; PTHR11280; GLUCOSAMINE-6-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR11280:SF5; GLUCOSAMINE-6-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF01182; Glucosamine_iso; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 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
//