AGAA2_SHESA
ID AGAA2_SHESA Reviewed; 394 AA.
AC A0KYQ5;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=N-acetylgalactosamine-6-phosphate deacetylase {ECO:0000303|PubMed:22711537};
DE Short=GalNAc-6-P deacetylase {ECO:0000303|PubMed:22711537};
DE EC=3.5.1.- {ECO:0000269|PubMed:22711537};
DE AltName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000303|PubMed:22711537};
DE Short=GlcNAc-6-P deacetylase {ECO:0000305|PubMed:22711537};
DE EC=3.5.1.25 {ECO:0000269|PubMed:22711537};
GN Name=agaAII {ECO:0000303|PubMed:22711537}; OrderedLocusNames=Shewana3_2697;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ANA-3;
RX PubMed=22711537; DOI=10.1074/jbc.m112.382333;
RA Leyn S.A., Gao F., Yang C., Rodionov D.A.;
RT "N-acetylgalactosamine utilization pathway and regulon in proteobacteria:
RT genomic reconstruction and experimental characterization in Shewanella.";
RL J. Biol. Chem. 287:28047-28056(2012).
CC -!- FUNCTION: Involved in the pathway of N-acetyl-D-galactosamine
CC degradation. Catalyzes the conversion of N-acetyl-D-galactosamine 6-
CC phosphate to D-galactosamine 6-phosphate and acetate. It can also
CC catalyze the conversion of N-acetyl-D-glucosamine 6-phosphate.
CC {ECO:0000269|PubMed:22711537}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-galactosamine 6-phosphate = acetate + D-
CC galactosamine 6-phosphate; Xref=Rhea:RHEA:18149, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:71673, ChEBI:CHEBI:71674;
CC Evidence={ECO:0000269|PubMed:22711537};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:22936, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=3.5.1.25;
CC Evidence={ECO:0000269|PubMed:22711537};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22711537}.
CC -!- MISCELLANEOUS: In Shewanella sp., the active phosphotransferase system
CC (PTS) specific for the transport of GalNAc and GalN is replaced by a
CC set of GalNAc- and GalN-specific permeases and kinases (AgaP and AgaK,
CC respectively). {ECO:0000305|PubMed:22711537}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC NagA family.
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DR EMBL; CP000469; ABK48924.1; -; Genomic_DNA.
DR RefSeq; WP_011717581.1; NC_008577.1.
DR AlphaFoldDB; A0KYQ5; -.
DR SMR; A0KYQ5; -.
DR STRING; 94122.Shewana3_2697; -.
DR EnsemblBacteria; ABK48924; ABK48924; Shewana3_2697.
DR KEGG; shn:Shewana3_2697; -.
DR eggNOG; COG1820; Bacteria.
DR HOGENOM; CLU_032482_2_2_6; -.
DR OMA; MFNHAPT; -.
DR OrthoDB; 1026967at2; -.
DR BioCyc; MetaCyc:MON-17511; -.
DR Proteomes; UP000002589; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047419; F:N-acetylgalactosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
DR CDD; cd00854; NagA; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR003764; GlcNAc_6-P_deAcase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11113:SF14; PTHR11113:SF14; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF038994; NagA; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR00221; nagA; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..394
FT /note="N-acetylgalactosamine-6-phosphate deacetylase"
FT /id="PRO_0000433129"
FT ACT_SITE 280
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 148..149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 225..226
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 254..257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 313..315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
SQ SEQUENCE 394 AA; 42410 MW; 1B81D3A886AFF68A CRC64;
MKPNTDFMLI ADGAKVLTQG NLTEHCAIEV SDGIICGLKS TISAEWTADK PHYRLTSGTL
VAGFIDTQVN GGGGLMFNHV PTLETLRLMM QAHRQFGTTA MLPTVITDDI EVMQAAADAV
AEAIDCQVPG IIGIHFEGPH LSVAKRGCHP PAHLRGITER EWLLYLRQDL GVRLITLAPE
SVTPEQIKRL VASGAIISLG HSNADGETVL KAIEAGASGF THLYNGMSAL TSREPGMVGA
AFASENTYCG IILDGQHVHP ISALAAWRAK GTEHLMLVTD AMSPLGSDQT EFQFFDGKVV
REGMTLRDQH GSLAGSVLDM ASAVRYAATE LNLGLSNAVQ MATRTPAEFI QRPQLGDIAE
GKQADWVWLD DDQRVLAVWI AGELLYQAEQ ARFA
