ID D3H695_STRM6 Unreviewed; 388 AA.
AC D3H695;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Tagatose-6-phosphate ketose/aldose isomerase {ECO:0000313|EMBL:CBJ21385.1};
DE EC=5.3.1.- {ECO:0000313|EMBL:CBJ21385.1};
GN Name=agaS {ECO:0000313|EMBL:CBJ21385.1};
GN OrderedLocusNames=smi_0084 {ECO:0000313|EMBL:CBJ21385.1};
OS Streptococcus mitis (strain B6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=365659 {ECO:0000313|EMBL:CBJ21385.1, ECO:0000313|Proteomes:UP000008563};
RN [1] {ECO:0000313|EMBL:CBJ21385.1, ECO:0000313|Proteomes:UP000008563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B6 {ECO:0000313|EMBL:CBJ21385.1,
RC ECO:0000313|Proteomes:UP000008563};
RX PubMed=20195536; DOI=10.1371/journal.pone.0009426;
RA Denapaite D., Brueckner R., Nuhn M., Reichmann P., Henrich B., Maurer P.,
RA Schaehle Y., Selbmann P., Zimmermann W., Wambutt R., Hakenbeck R.;
RT "The genome of Streptococcus mitis B6--what is a commensal?";
RL PLoS ONE 5:E9426-E9426(2010).
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}.
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DR EMBL; FN568063; CBJ21385.1; -; Genomic_DNA.
DR RefSeq; WP_000903539.1; NC_013853.1.
DR RefSeq; YP_003445255.1; NC_013853.1.
DR AlphaFoldDB; D3H695; -.
DR STRING; 365659.smi_0084; -.
DR KEGG; smb:smi_0084; -.
DR PATRIC; fig|365659.3.peg.85; -.
DR eggNOG; COG2222; Bacteria.
DR HOGENOM; CLU_012520_0_0_9; -.
DR OrthoDB; 9779207at2; -.
DR Proteomes; UP000008563; Chromosome.
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 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:CBJ21385.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 42..202
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 221..368
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 388 AA; 42962 MW; 24292F7E7B1C5A60 CRC64;
MLHYTKEDLL ELGAEITTRE IYQQPDVWKE AFESYQEQRE EIAAFLQGIA DKHDYIKVIL
TGAGTSAYVG DTLVPYFKEV YDERKWNFNA IATTDIVANP ETYLKKDVAT VLVSFARSGN
SPESVATVDL AKALVDELYQ VTITCASDGK LALQAHGDDR NLLLLQPAAS NDAGFAMTSS
FTSMMLTALL VFDPTEFAVK AERFEVVSSL ARKVLDKAED VKELVDLDFN RVIYLGAGPF
FGLAHEAQLK ILELTAGQVA TMYESPVGFR HGPKSLINED TVVLVFGTTT DYTRKYDLDL
VREVAGDQIA RRVVLLSDQA FGLENVKEVA LGCGGVLNDI YRVFPYIVYA QLFALLTSLK
VENKPDTPSP TGTVNRVVQG VIIHDYQK
//
