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N-acetylgalactosamine-6-phosphate deacetylase (GalNAc-6-P deacetylase) (EC 3.5.1.-) (N-acetylglucosamine-6-phosphate deacetylase) (GlcNAc-6-P deacetylase) (EC 3.5.1.25)

 AGAA2_SHESA             Reviewed;         394 AA.
A0KYQ5;
27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 1.
05-JUL-2017, entry version 66.
RecName: Full=N-acetylgalactosamine-6-phosphate deacetylase {ECO:0000303|PubMed:22711537};
Short=GalNAc-6-P deacetylase {ECO:0000303|PubMed:22711537};
EC=3.5.1.- {ECO:0000269|PubMed:22711537};
AltName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000303|PubMed:22711537};
Short=GlcNAc-6-P deacetylase {ECO:0000305|PubMed:22711537};
EC=3.5.1.25 {ECO:0000269|PubMed:22711537};
Name=agaAII {ECO:0000303|PubMed:22711537};
OrderedLocusNames=Shewana3_2697;
Shewanella sp. (strain ANA-3).
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Shewanellaceae; Shewanella.
NCBI_TaxID=94122;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ANA-3;
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J.,
Tiedje J., Richardson P.;
"Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
STRAIN=ANA-3;
PubMed=22711537; DOI=10.1074/jbc.M112.382333;
Leyn S.A., Gao F., Yang C., Rodionov D.A.;
"N-acetylgalactosamine utilization pathway and regulon in
proteobacteria: genomic reconstruction and experimental
characterization in Shewanella.";
J. Biol. Chem. 287:28047-28056(2012).
-!- FUNCTION: Involved in the pathway of N-acetyl-D-galactosamine
degradation. Catalyzes the conversion of N-acetyl-D-galactosamine
6-phosphate to D-galactosamine 6-phosphate and acetate. It can
also catalyze the conversion of N-acetyl-D-glucosamine 6-
phosphate. {ECO:0000269|PubMed:22711537}.
-!- CATALYTIC ACTIVITY: N-acetyl-D-galactosamine 6-phosphate + H(2)O =
D-galactosamine 6-phosphate + acetate.
{ECO:0000269|PubMed:22711537}.
-!- CATALYTIC ACTIVITY: N-acetyl-D-glucosamine 6-phosphate + H(2)O =
D-glucosamine 6-phosphate + acetate.
{ECO:0000269|PubMed:22711537}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22711537}.
-!- MISCELLANEOUS: In Shewanella sp., the active phosphotransferase
system (PTS) specific for the transport of GalNAc and GalN is
replaced by a set of GalNAc- and GalN-specific permeases and
kinases (AgaP and AgaK, respectively).
{ECO:0000305|PubMed:22711537}.
-!- SIMILARITY: Belongs to the metallo-dependent hydrolases
superfamily. NagA family.
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EMBL; CP000469; ABK48924.1; -; Genomic_DNA.
RefSeq; WP_011717581.1; NC_008577.1.
ProteinModelPortal; A0KYQ5; -.
SMR; A0KYQ5; -.
STRING; 94122.Shewana3_2697; -.
EnsemblBacteria; ABK48924; ABK48924; Shewana3_2697.
KEGG; shn:Shewana3_2697; -.
eggNOG; ENOG4105CE4; Bacteria.
eggNOG; COG1820; LUCA.
HOGENOM; HOG000275008; -.
KO; K01443; -.
OMA; YCGIILD; -.
OrthoDB; POG091H03KA; -.
BioCyc; MetaCyc:MONOMER-17511; -.
Proteomes; UP000002589; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
CDD; cd00854; NagA; 1.
Gene3D; 2.30.40.10; -; 1.
InterPro; IPR006680; Amidohydro-rel.
InterPro; IPR003764; GlcNAc_6-P_deAcase.
InterPro; IPR011059; Metal-dep_hydrolase_composite.
InterPro; IPR032466; Metal_Hydrolase.
Pfam; PF01979; Amidohydro_1; 1.
PIRSF; PIRSF038994; NagA; 1.
SUPFAM; SSF51338; SSF51338; 2.
SUPFAM; SSF51556; SSF51556; 1.
TIGRFAMs; TIGR00221; nagA; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase;
Metal-binding; Zinc.
CHAIN 1 394 N-acetylgalactosamine-6-phosphate
deacetylase.
/FTId=PRO_0000433129.
REGION 148 149 Substrate binding.
{ECO:0000250|UniProtKB:P0AF18}.
REGION 225 226 Substrate binding.
{ECO:0000250|UniProtKB:P0AF18}.
REGION 254 257 Substrate binding.
{ECO:0000250|UniProtKB:P0AF18}.
REGION 313 315 Substrate binding.
{ECO:0000250|UniProtKB:P0AF18}.
ACT_SITE 280 280 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P0AF18}.
METAL 137 137 Zinc. {ECO:0000250|UniProtKB:P0AF18}.
METAL 201 201 Zinc; via tele nitrogen.
{ECO:0000250|UniProtKB:P0AF18}.
METAL 222 222 Zinc; via tele nitrogen.
{ECO:0000250|UniProtKB:P0AF18}.
BINDING 233 233 Substrate.
{ECO:0000250|UniProtKB:P0AF18}.
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


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