ID   AGAS_SHESA              Reviewed;         386 AA.
AC   A0KYQ7;
DT   27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=D-galactosamine-6-phosphate deaminase AgaS {ECO:0000303|PubMed:22711537};
DE            Short=GalN-6-P deaminase {ECO:0000303|PubMed:22711537};
DE            EC=3.5.99.- {ECO:0000269|PubMed:22711537};
DE   AltName: Full=Glucosamine-6-phosphate deaminase {ECO:0000303|PubMed:22711537};
DE            Short=GlcN-6-P deaminase {ECO:0000305|PubMed:22711537};
DE            EC=3.5.99.6 {ECO:0000269|PubMed:22711537};
GN   Name=agaS {ECO:0000303|PubMed:22711537}; OrderedLocusNames=Shewana3_2699;
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 {ECO:0000312|Proteomes:UP000002589};
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 D-galactosamine 6-phosphate
CC       (GalN-6-P) to D-tagatofuranose 6-phosphate (Tag-6-P). It can also
CC       catalyze the conversion of D-glucosamine 6-phosphate.
CC       {ECO:0000269|PubMed:22711537}.
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:0000269|PubMed:22711537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-
CC         phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6;
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 SIS family. AgaS subfamily. {ECO:0000305}.
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DR   EMBL; CP000469; ABK48926.1; -; Genomic_DNA.
DR   RefSeq; WP_011717583.1; NC_008577.1.
DR   AlphaFoldDB; A0KYQ7; -.
DR   SMR; A0KYQ7; -.
DR   STRING; 94122.Shewana3_2699; -.
DR   EnsemblBacteria; ABK48926; ABK48926; Shewana3_2699.
DR   KEGG; shn:Shewana3_2699; -.
DR   eggNOG; COG2222; Bacteria.
DR   HOGENOM; CLU_012520_0_0_6; -.
DR   OMA; YHLIITC; -.
DR   OrthoDB; 1046291at2; -.
DR   BioCyc; MetaCyc:MON-17512; -.
DR   Proteomes; UP000002589; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004342; F:glucosamine-6-phosphate deaminase 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; 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   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Hydrolase; Repeat.
FT   CHAIN           1..386
FT                   /note="D-galactosamine-6-phosphate deaminase AgaS"
FT                   /id="PRO_0000433130"
FT   DOMAIN          59..217
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   DOMAIN          222..366
FT                   /note="SIS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
SQ   SEQUENCE   386 AA;  42692 MW;  8D3833E9C623C671 CRC64;
     MLTSPLSPFE HEDSNLLLSA EQLTQYGAFW TAKEISQQPK MWRKVSEQHS DNRTIAAWLT
     PILAKPQLRI ILTGAGTSAY IGDVLAAHIQ QHLPLATQQV EAISTTDIVS HPELYLRGNI
     PTLLISYGRS GNSPESMAAV ELAEQLVDDC YHLAITCNGQ GKLANYCADK SHCYLYKLPD
     ETHDVSFAMT SSFTCMYLAT LLIFAPNSQA LMQCIEMAEH ILTERLADIR LQSEQPSKRV
     VFLGGGPLKA IAQEAALKYL ELTAGQVVSA FESPLGFRHG PKSLVDSHTQ VLVMMSSDPY
     TRQYDNDLIQ ELKRDNQALS VLTLSEELLT GSSGLNEVWL GLPFILWCQI LAIYKAIQLK
     VSPDNPCPTG QVNRVVQGVN VYPFVK