ID   GAHP1_LACP7             Reviewed;         724 AA.
AC   A9KQ75;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=1,3-beta-galactosyl-N-acetylhexosamine phosphorylase Cphy3030;
DE            EC=2.4.1.211;
DE   AltName: Full=D-galactosyl-1,4-L-rhamnose phosphorylase;
GN   OrderedLocusNames=Cphy_3030;
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:ABX43387.1}
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-galactopyranosyl-(1->3)-N-
CC       acetyl-D-glucosamine to form alpha-D-galactopyranose 1-phosphate and
CC       acetyl-D-glucosamine. Active towards galacto-N-biose and lacto-N-biose.
CC       Does not phosphorolyze galacto-N-tetraose or lacto-N-tetraose. In the
CC       reverse reaction has activity toward N-acetyl-D-glucosamine and N-
CC       acetyl-D-galactosamine, but not L-rhamnose, D-glucose or D-galactose.
CC       {ECO:0000269|PubMed:19491100}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine + phosphate =
CC         alpha-D-galactose 1-phosphate + N-acetyl-D-glucosamine;
CC         Xref=Rhea:RHEA:20285, ChEBI:CHEBI:27707, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58336, ChEBI:CHEBI:506227; EC=2.4.1.211;
CC         Evidence={ECO:0000269|PubMed:19491100};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.8 mM for lacto-N-biose {ECO:0000269|PubMed:19491100};
CC         KM=10 mM for galacto-N-biose {ECO:0000269|PubMed:19491100};
CC         KM=1.9 mM for N-acetyl-D-glucosamine {ECO:0000269|PubMed:19491100};
CC         KM=3.3 mM for N-acetyl-D-galactosamine {ECO:0000269|PubMed:19491100};
CC   -!- SIMILARITY: Belongs to the glycoside hydrolase 112 family.
CC       {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; CP000885; ABX43387.1; -; Genomic_DNA.
DR   RefSeq; WP_012201038.1; NC_010001.1.
DR   AlphaFoldDB; A9KQ75; -.
DR   SMR; A9KQ75; -.
DR   STRING; 357809.Cphy_3030; -.
DR   CAZy; GH112; Glycoside Hydrolase Family 112.
DR   EnsemblBacteria; ABX43387; ABX43387; Cphy_3030.
DR   KEGG; cpy:Cphy_3030; -.
DR   eggNOG; COG5426; Bacteria.
DR   HOGENOM; CLU_022367_0_0_9; -.
DR   OMA; PMHEYTV; -.
DR   OrthoDB; 205469at2; -.
DR   BRENDA; 2.4.1.211; 10424.
DR   Proteomes; UP000000370; Chromosome.
DR   GO; GO:0050500; F:1,3-beta-galactosyl-N-acetylhexosamine phosphorylase activity; IDA:UniProtKB.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR013780; Glyco_hydro_b.
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   Transferase.
FT   CHAIN           1..724
FT                   /note="1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
FT                   Cphy3030"
FT                   /id="PRO_0000405290"
FT   ACT_SITE        316
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   724 AA;  83856 MW;  B8C569DA5949169B CRC64;
     MSEKLTGRVT VPTDVDMIQE TKEIAERWGA DALRDCDGTD MPDELKKMPA KIYSTYYTTR
     KDNAWANANP DEVQQVYLMT EFYTAMSQGE LRIPLMKHLY KDQLKPNTIH DIKRWWEVVD
     RTTGEPLVLD AWEYDENNQE VIILNPDHFH DYTVSFLAFI IWDPVHMYNF ITNDWQDVEH
     QITYDVRQPK TQKYVIEKLK RWMKENPDSD VVRFTTFFHQ FTLVFNEFAK EKFVDWFGYS
     ASVSPYILEQ FEKEVGYKFR PEYIIDQGYH NNTNRVPSKE FRDFQEFQQR EVAKLMKVLV
     DICHDNDKEA MMFLGDHWIG TEPFGEYFKH VGLDAVVGSV GNGTTLRLIS DIPGVKYTEG
     RFLPYFFPDV FHEGGDPIKE AKVNWVTARR AILRKPVDRI GYGGYLKLAL DFPEFIQYIE
     EVCDEFRLLY DNMGGQSPYS HFKVGVLNSW GKIRSWGTHM VAHAIDYKQT YSYAGVLEAL
     SGMPFDVEFI SFEDVIKNPV ILNECGVVIN VGDAYTGPSG GAYWTNEKVS SAVKAFVAQG
     GGFIGVGEPS ACEHQGRYFT LANVLGVNKE IGFSMSTDKY NWDEHSHFIT EDSNESINFG
     EGMKNIYALD GAQILRKDGQ DVQMAVNQFG DGRSVYISGI PYSFENSRML YRAIFWAAGM
     EQEMKKWYSS NYNVEVNYYP ATKKYCIVNN TYEPQETMIY DGLGREYSMK LKANDILWFT
     FLED