ID   GLRP_LACP7              Reviewed;         722 AA.
AC   A9KHK4;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=D-galactosyl-beta-1->4-L-rhamnose phosphorylase {ECO:0000303|PubMed:19491100};
DE            EC=2.4.1.247;
GN   OrderedLocusNames=Cphy_1920;
OS   Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS   (Clostridium phytofermentans).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=357809;
RN   [1] {ECO:0000312|EMBL:ABX42289.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA   Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA   LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT   "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19491100; DOI=10.1074/jbc.m109.007666;
RA   Nakajima M., Nishimoto M., Kitaoka M.;
RT   "Characterization of three beta-galactoside phosphorylases from Clostridium
RT   phytofermentans: discovery of d-galactosyl-beta1->4-l-rhamnose
RT   phosphorylase.";
RL   J. Biol. Chem. 284:19220-19227(2009).
CC   -!- FUNCTION: Reversibly phosphorolyzes beta-D-galactosyl-(1->4)-L-rhamnose
CC       to form alpha-D-galactose 1-phosphate and L-rhamnose. Does not
CC       phosphorolyze galacto-N-biose or lacto-N-biose. In the reverse
CC       reaction, has the highest activity toward L-rhamnose, also has activity
CC       toward L-mannose, and low activity toward L-lyxose, D-glucose, 2-deoxy-
CC       D-glucose and D-galactose. {ECO:0000269|PubMed:19491100}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-galactosyl-(1->4)-L-rhamnose + phosphate = alpha-D-
CC         galactose 1-phosphate + L-rhamnopyranose; Xref=Rhea:RHEA:26474,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:55332, ChEBI:CHEBI:58336,
CC         ChEBI:CHEBI:62346; EC=2.4.1.247;
CC         Evidence={ECO:0000269|PubMed:19491100};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.4 mM for L-rhamnose {ECO:0000269|PubMed:19491100};
CC         KM=78 mM for L-mannose {ECO:0000269|PubMed:19491100};
CC         KM=7.9 mM for beta-D-galactosyl-(1->4)-L-rhamnose
CC         {ECO:0000269|PubMed:19491100};
CC   -!- SIMILARITY: Belongs to the glycoside hydrolase 112 family.
CC       {ECO:0000305}.
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DR   EMBL; CP000885; ABX42289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9KHK4; -.
DR   SMR; A9KHK4; -.
DR   STRING; 357809.Cphy_1920; -.
DR   CAZy; GH112; Glycoside Hydrolase Family 112.
DR   EnsemblBacteria; ABX42289; ABX42289; Cphy_1920.
DR   KEGG; cpy:Cphy_1920; -.
DR   eggNOG; COG5426; Bacteria.
DR   HOGENOM; CLU_022367_0_0_9; -.
DR   OMA; GHFHETY; -.
DR   BioCyc; MetaCyc:MON-15015; -.
DR   BRENDA; 2.4.1.247; 10424.
DR   Proteomes; UP000000370; Chromosome.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR   GO; GO:0019299; P:rhamnose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR035080; Lact_bio_phlase-like_N.
DR   InterPro; IPR012711; Lacto-N-biose_phosphorylase.
DR   InterPro; IPR035356; LBP_C.
DR   InterPro; IPR035363; LBP_M.
DR   Pfam; PF09508; Lact_bio_phlase; 1.
DR   Pfam; PF17386; LBP_C; 1.
DR   Pfam; PF17385; LBP_M; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR02336; TIGR02336; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW   Rhamnose metabolism; Transferase.
FT   CHAIN           1..722
FT                   /note="D-galactosyl-beta-1->4-L-rhamnose phosphorylase"
FT                   /id="PRO_0000405292"
FT   ACT_SITE        319
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   722 AA;  83279 MW;  897574E1F1AE970C CRC64;
     MEQQKEITKG GFTLPGEAGF EKLTLELANR WGADVIRDSD GTELSDDILN AGYGIYSTIC
     LIRDHNAWAK ANIDKLQQTF LVTSPVVANS ETLTIDLMEG FFKEQFLVND SEEALEYWQV
     YDRTTETLLQ KESWSYHPQN QTVVLTGICP WHKYTVSFMA YRIWEEISMY NHTTNNWNKE
     HLMQIDPIHK ETQEYLLTWM DDWCKKHEQT TVVRFTSMFY NFVWMWGSNE KNRYLFSDWA
     SYDFTVSPHA LKLFEEEYGY VLTAEDFIHQ GKFHVTHMPA DKHKLDWMEF INNFVVDFGK
     KLIDIVHNYG KLAYVFYDDS WVGVEPYHKN FEKFGFDGLI KCVFSGFEVR LCAGVKVNTH
     ELRLHPYLFP VGLGGAPTFM EGGNPTLDAK NYWISVRRAL LREPIDRIGL GGYLHLVEDF
     PDFTDYIEKI ANEFRRIKEL HNAGKPMALK PRIAVLHSWG SLRSWTLSGH FHETYMHDLI
     HINESLSGLP FDVKFINFED INQGALEEVD VVINAGIMGS AWTGGQAWED QEIIERLTRF
     VYEGKAFIGV NEPSALTGYD TLYRMAHVLG VDMDLGDRVS HGRYSFTEEP VEELEFAECG
     PKAKRNIYLT DGLAKVLKEE NGIPVMTSYE FGRGRGIYLA SYEHSIKNAR TLLNIILYAA
     GESFHQEGIT NNVYTECAYY EKDKILVMIN NSNTLQESSV TIKGRTYTKD IPAFDTVILP
     LE