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Database: UniProt
Entry: A0A0C1Y431_9ACTN
LinkDB: A0A0C1Y431_9ACTN
Original site: A0A0C1Y431_9ACTN 
ID   A0A0C1Y431_9ACTN        Unreviewed;       392 AA.
AC   A0A0C1Y431;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Tagatose-6-phosphate ketose isomerase {ECO:0000313|EMBL:KIF75312.1};
GN   ORFNames=QR77_18075 {ECO:0000313|EMBL:KIF75312.1};
OS   Streptomyces sp. 150FB.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF75312.1, ECO:0000313|Proteomes:UP000031584};
RN   [1] {ECO:0000313|EMBL:KIF75312.1, ECO:0000313|Proteomes:UP000031584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=150FB {ECO:0000313|EMBL:KIF75312.1,
RC   ECO:0000313|Proteomes:UP000031584};
RA   Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT   "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT   150.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00029292};
CC   -!- SIMILARITY: Belongs to the SIS family. AgaS subfamily.
CC       {ECO:0000256|ARBA:ARBA00007748}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIF75312.1}.
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DR   EMBL; JTHL01000001; KIF75312.1; -; Genomic_DNA.
DR   RefSeq; WP_040022939.1; NZ_JTHL01000001.1.
DR   AlphaFoldDB; A0A0C1Y431; -.
DR   STRING; 1576605.QR77_18075; -.
DR   OrthoDB; 9779207at2; -.
DR   Proteomes; UP000031584; Unassembled WGS sequence.
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:UniProtKB-KW.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
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   NCBIfam; TIGR02815; agaS_fam; 1.
DR   PANTHER; PTHR32502:SF3; D-GALACTOSAMINE-6-PHOSPHATE DEAMINASE AGAS-RELATED; 1.
DR   PANTHER; PTHR32502; N-ACETYLGALACTOSAMINE PERMEASE II COMPONENT-RELATED; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Isomerase {ECO:0000313|EMBL:KIF75312.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031584};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          46..206
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          217..372
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   392 AA;  40625 MW;  84F40782DB9CBB50 CRC64;
     MTSPSSTPPT DDGAANTVRE IAQQPRLWRE VGQLVAASRD SLDTFLRPLT ARGDLRVVLT
     GAGTSAYAGQ VLQAGLARRL GLRVDAVATT DLVADPRGCL AEDVPTLLVS FARSGDSPES
     VAAADLADQV LTEVHHLVIT CNEQGALALN HADRPTSHVL LMPAAANDQG FAMTSSFTCM
     TLAALLALGG GAYDGIAERL ADAAELILKD GAADRAIGDL VGRAPERIVY LGSGALKGLA
     EESALKVLEL TGGTVVAVAD SSMGFRHGPK AVLNDRTVVV VYVSNDPYTR QYDEDIVAEL
     RGNLPGGRVV TVAAGALRAS ATDPEAGADV GTWPLPGLDD VDDVALALPA VVYAQLIALR
     ASLAGGIRPD QPFPSGEVNR VVRGVILHPL AR
//
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