ID   GAHP2_LACP7             Reviewed;         723 AA.
AC   A9KIW5;
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 Cphy0577;
DE            EC=2.4.1.211;
DE   AltName: Full=D-galactosyl-1,4-L-rhamnose phosphorylase;
GN   OrderedLocusNames=Cphy_0577;
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:ABX40964.1}
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=4.5 mM for lacto-N-biose {ECO:0000269|PubMed:19491100};
CC         KM=8.0 mM for galacto-N-biose {ECO:0000269|PubMed:19491100};
CC         KM=3.4 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}.
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DR   EMBL; CP000885; ABX40964.1; -; Genomic_DNA.
DR   RefSeq; WP_012198608.1; NC_010001.1.
DR   AlphaFoldDB; A9KIW5; -.
DR   SMR; A9KIW5; -.
DR   STRING; 357809.Cphy_0577; -.
DR   CAZy; GH112; Glycoside Hydrolase Family 112.
DR   EnsemblBacteria; ABX40964; ABX40964; Cphy_0577.
DR   KEGG; cpy:Cphy_0577; -.
DR   eggNOG; COG5426; Bacteria.
DR   HOGENOM; CLU_022367_0_0_9; -.
DR   OMA; LYRSILW; -.
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..723
FT                   /note="1,3-beta-galactosyl-N-acetylhexosamine phosphorylase
FT                   Cphy0577"
FT                   /id="PRO_0000405291"
FT   ACT_SITE        317
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   723 AA;  83896 MW;  9ABCB04396E01B35 CRC64;
     MKKDTMLAGR VTIPTDVDVV PETMELLNRW GADAIRDCDG TDYPEELKAV QAKVYSTYYT
     TRKDNAWAKA HPEEVQQCYI MTSFYTATET TLRIPLLKGI AKELMMVNNY DDKVRWWEVI
     DRSTAMVVST DTWSYDKETG EVIITNCEPF HNYTVSFLAY LIWDPVHMYN AVVNGWQGVE
     HQITFDVRQP KTREYSMVRL RKFIEEHPYV DVIRYTTFFH QFTLVFDEMM REKYVDWYGY
     SASVSPYILE QFEKEVGYRF RPEFIIDQGY YNNQYRIPSK EFKDFQAFQR REVAKLAKEM
     VDITHEYGKE AMMFLGDHWI GTEPFMEEFK TIGLDAVVGS VGNGSTLRLI SDIPGVKYTE
     GRFLPYFFPD TFHEGGDPVK EAKVNWVTAR RAILRKPIDR IGYGGYLKLA CQFPEFIDYV
     ESVCNEFREL YENIKGTTPF CIKRVAVLNS WGKMRAWGAH MVHHALYQKQ NYSYAGVIES
     LSGTPFEVSF ISFDDIKKDK NILKNIDVII NVGDGDTAHT GGLVWEDADI SSAIHQFVYE
     GGGLIGIGEP TGHQYQGRYI QLANVFGIEK ETGFTLNYDK YNWDAVESHF ITEDCTKEVD
     FGEGKKNMYA LEGTTILVQM EKEVQMAVNE FGKGRSVYLS GLPYSFENSR VLYRSILWSA
     HEEENLHKWY SSNFNVEVHA YVKNNKYCVV NNTYEPQNTT IYRGDSSSFD LELEANEIIW
     YEI