ID A0A0R1KF51_9LACO Unreviewed; 389 AA.
AC A0A0R1KF51;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Phosphosugar isomerase {ECO:0000313|EMBL:KRK79057.1};
GN ORFNames=FD03_GL001420 {ECO:0000313|EMBL:KRK79057.1};
OS Companilactobacillus nodensis DSM 19682 = JCM 14932 = NBRC 107160.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1423775 {ECO:0000313|EMBL:KRK79057.1, ECO:0000313|Proteomes:UP000051248};
RN [1] {ECO:0000313|EMBL:KRK79057.1, ECO:0000313|Proteomes:UP000051248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19682 {ECO:0000313|EMBL:KRK79057.1,
RC ECO:0000313|Proteomes:UP000051248};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRK79057.1}.
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DR EMBL; AZDZ01000019; KRK79057.1; -; Genomic_DNA.
DR RefSeq; WP_025024955.1; NZ_BCWC01000001.1.
DR AlphaFoldDB; A0A0R1KF51; -.
DR STRING; 1423775.FD03_GL001420; -.
DR PATRIC; fig|1423775.4.peg.1449; -.
DR eggNOG; COG2222; Bacteria.
DR OrthoDB; 9779207at2; -.
DR Proteomes; UP000051248; 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 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; 1.
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:KRK79057.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 50..203
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 221..370
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 389 AA; 42599 MW; 845018E2E69264D4 CRC64;
MFSKTDKELE EMGAQITTRE IQQQPDLWKE AYDNFVGNQD QVNNFLDEII SNFPDKKIRV
IFTGAGTSAY VGDTLRPYLN KVGDTSHFNF ETIPTTDIVS APLDNLRADD PTILVSFARS
GNSPESVATV ELAEKIIKNL YQITITCAPE GHLAKKAKNE DGNLLLLQPA GSNDKGFAMT
GSFSCMTLTA ALIFDQSVAD KKPWIDAIVK MGQEVVSRES EIQAIADLDY DRIAYLGTGS
LSGLTREAQL KVLELTAGQL TTIFDSSMGF RHGPKSYVNG KTVVFDFLSN DKYSRQYDVD
ILEEIKGDEI CKKVIGVGTS ADNNFSGDNF LIQAGLPDLP ELYQALPDVM FAQTFALLSS
IKVGNTPDTP SASGTVNRVV KGVTIHDYE
//
