ID   AGAS_STRCO              Reviewed;         385 AA.
AC   O50523;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Putative D-galactosamine-6-phosphate deaminase AgaS {ECO:0000305};
DE            EC=3.5.99.- {ECO:0000250|UniProtKB:Q9KIP9};
DE   AltName: Full=Gam-6-P deaminase/isomerase {ECO:0000250|UniProtKB:Q9KIP9};
GN   Name=agaS; OrderedLocusNames=SCO5849; ORFNames=SC9B10.16;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Catalyzes the isomerization-deamination of galactosamine 6-
CC       phosphate to form tagatofuranose 6-phosphate and ammonium ion.
CC       {ECO:0000250|UniProtKB:Q9KIP9}.
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:0000250|UniProtKB:Q9KIP9};
CC   -!- SIMILARITY: Belongs to the SIS family. AgaS subfamily. {ECO:0000305}.
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; AL939125; CAA15806.1; -; Genomic_DNA.
DR   PIR; T35885; T35885.
DR   RefSeq; NP_629972.1; NC_003888.3.
DR   RefSeq; WP_011030496.1; NZ_VNID01000007.1.
DR   AlphaFoldDB; O50523; -.
DR   SMR; O50523; -.
DR   STRING; 100226.SCO5849; -.
DR   PRIDE; O50523; -.
DR   GeneID; 1101291; -.
DR   KEGG; sco:SCO5849; -.
DR   PATRIC; fig|100226.15.peg.5948; -.
DR   eggNOG; COG2222; Bacteria.
DR   HOGENOM; CLU_012520_0_0_11; -.
DR   InParanoid; O50523; -.
DR   OMA; YHLIITC; -.
DR   PhylomeDB; O50523; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:InterPro.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
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   InterPro; IPR014180; Sugar_isomerase_AgaS.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   TIGRFAMs; TIGR02815; agaS_fam; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Reference proteome; Repeat.
FT   CHAIN           1..385
FT                   /note="Putative D-galactosamine-6-phosphate deaminase AgaS"
FT                   /id="PRO_0000136591"
FT   DOMAIN          46..206
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   DOMAIN          217..365
FT                   /note="SIS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
SQ   SEQUENCE   385 AA;  40446 MW;  91497CEE0805F8A7 CRC64;
     MTTPPGTLPV DDSAVHTVRE IAQQPALWRE VDRIVGASRE ALDAFLDPLV ARGDLRVVLT
     GAGTSAFAGQ VLQPSLARHL GRRVDAVPTT DLVADPRGCL AEDLPTLLVS FARSGDSPES
     VAATALADQV LSEVHHLVIT CNEQGRLARE HTRRPRSHVL LMPAASNDRG FAMTSSFTCM
     TLAALLALGK DARDGVAERL ARAAESIIED GAADRTAGAL VDRAPERIVF LGSGPLKGLA
     EESALKVLEL TGGTLMAVAE SSLGFRHGPK AVLNERSVAV VYVSNDPYTR RYDHDIVAEL
     RGNLPVGSVV AVSAESGAGT EGADAWPLPG LGDVEDAALA LPAVVYAQLI ALRASQARGL
     RPDNPFPSGE VNRVVQGVTL HSLND