LNPA_BIFL2
ID LNPA_BIFL2 Reviewed; 751 AA.
AC E8MF13; Q5NU17;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=1,3-beta-galactosyl-N-acetylhexosamine phosphorylase;
DE EC=2.4.1.211;
DE AltName: Full=Galacto-N-biose/lacto-N-biose I phosphorylase;
DE Short=GLNBP;
GN Name=lnpA; Synonyms=lnbp; OrderedLocusNames=BLLJ_1623;
OS Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM
OS 1217 / NCTC 11818 / E194b).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=565042;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND GENE
RP NAME.
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=15933016; DOI=10.1128/aem.71.6.3158-3162.2005;
RA Kitaoka M., Tian J., Nishimoto M.;
RT "Novel putative galactose operon involving lacto-N-biose phosphorylase in
RT Bifidobacterium longum.";
RL Appl. Environ. Microbiol. 71:3158-3162(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=17720833; DOI=10.1128/aem.01425-07;
RA Nishimoto M., Kitaoka M.;
RT "Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-
RT biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum.";
RL Appl. Environ. Microbiol. 73:6444-6449(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-751 IN COMPLEX WITH
RP N-ACETYLGLUCOSAMINE AND N-ACETYLGALACTOSAMINE, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF ARG-32; ASN-166;
RP ARG-210; ARG-358; TYR-362 AND PHE-364.
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=19124470; DOI=10.1074/jbc.m808525200;
RA Hidaka M., Nishimoto M., Kitaoka M., Wakagi T., Shoun H., Fushinobu S.;
RT "The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a
RT large deformation of a TIM barrel scaffold.";
RL J. Biol. Chem. 284:7273-7283(2009).
CC -!- FUNCTION: Reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-
CC acetylglucosamine (GlcNAc) and galacto-N-biose to Gal1-P and N-
CC acetylgalactosamine (GalNAc). Involved in the lacto-N-biose I/galacto-
CC N-biose (LNB/GNB) degradation pathway, which is important for host
CC intestinal colonization by bifidobacteria.
CC {ECO:0000269|PubMed:15933016, ECO:0000269|PubMed:17720833,
CC ECO:0000269|PubMed:19124470}.
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:15933016, ECO:0000269|PubMed:19124470};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19124470}.
CC -!- SIMILARITY: Belongs to the glycoside hydrolase 112 family.
CC {ECO:0000305}.
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DR EMBL; AB181926; BAD80751.1; -; Genomic_DNA.
DR EMBL; AB303839; BAF73924.1; -; Genomic_DNA.
DR EMBL; AP010888; BAJ67290.1; -; Genomic_DNA.
DR RefSeq; WP_007056738.1; NC_015067.1.
DR PDB; 2ZUS; X-ray; 2.11 A; A/B/C/D=1-751.
DR PDB; 2ZUT; X-ray; 1.90 A; A/B/C/D=1-751.
DR PDB; 2ZUU; X-ray; 2.30 A; A/B/C/D=1-751.
DR PDB; 2ZUV; X-ray; 1.85 A; A/B=1-751.
DR PDB; 2ZUW; X-ray; 2.11 A; A/B/C/D=1-751.
DR PDB; 3WFZ; X-ray; 2.60 A; A/B/C/D=1-751.
DR PDBsum; 2ZUS; -.
DR PDBsum; 2ZUT; -.
DR PDBsum; 2ZUU; -.
DR PDBsum; 2ZUV; -.
DR PDBsum; 2ZUW; -.
DR PDBsum; 3WFZ; -.
DR AlphaFoldDB; E8MF13; -.
DR SMR; E8MF13; -.
DR CAZy; GH112; Glycoside Hydrolase Family 112.
DR PRIDE; E8MF13; -.
DR KEGG; blm:BLLJ_1623; -.
DR HOGENOM; CLU_022367_0_0_11; -.
DR OMA; PMHEYTV; -.
DR BRENDA; 2.4.1.211; 851.
DR GO; GO:0050500; F:1,3-beta-galactosyl-N-acetylhexosamine phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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 3D-structure; Carbohydrate metabolism; Glycosyltransferase; Transferase.
FT CHAIN 1..751
FT /note="1,3-beta-galactosyl-N-acetylhexosamine
FT phosphorylase"
FT /id="PRO_0000424070"
FT ACT_SITE 313
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:19124470"
FT MUTAGEN 32
FT /note="R->E: Lack of activity."
FT /evidence="ECO:0000269|PubMed:19124470"
FT MUTAGEN 166
FT /note="N->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:19124470"
FT MUTAGEN 210
FT /note="R->E: Lack of activity."
FT /evidence="ECO:0000269|PubMed:19124470"
FT MUTAGEN 358
FT /note="R->E: Lack of activity."
FT /evidence="ECO:0000269|PubMed:19124470"
FT MUTAGEN 362
FT /note="Y->F: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:19124470"
FT MUTAGEN 362
FT /note="Y->N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:19124470"
FT MUTAGEN 364
FT /note="F->N: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:19124470"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:2ZUV"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:2ZUV"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 148..157
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 186..201
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:2ZUV"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 276..302
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 306..314
FT /evidence="ECO:0007829|PDB:2ZUV"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 351..361
FT /evidence="ECO:0007829|PDB:2ZUV"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 375..391
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 410..430
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 439..447
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 448..451
FT /evidence="ECO:0007829|PDB:2ZUV"
FT TURN 452..456
FT /evidence="ECO:0007829|PDB:2ZUV"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 468..478
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 480..488
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 489..495
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:2ZUV"
FT TURN 513..515
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 517..521
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 523..534
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 538..544
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 547..552
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 560..563
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 564..567
FT /evidence="ECO:0007829|PDB:2ZUV"
FT TURN 587..591
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 596..605
FT /evidence="ECO:0007829|PDB:2ZUV"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 635..639
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 642..646
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:2ZUW"
FT STRAND 653..659
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 662..668
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 674..687
FT /evidence="ECO:0007829|PDB:2ZUV"
FT HELIX 691..694
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 698..701
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 704..709
FT /evidence="ECO:0007829|PDB:2ZUV"
FT TURN 710..713
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 714..719
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 725..730
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 736..741
FT /evidence="ECO:0007829|PDB:2ZUV"
FT STRAND 746..749
FT /evidence="ECO:0007829|PDB:2ZUV"
SQ SEQUENCE 751 AA; 84327 MW; E2C4E2471C6761EB CRC64;
MTSTGRFTLP SEENFAEKTK ELAELWGADA IRNSDGTHLD EAVLALGKKI YNAYFPTRAH
NEWITLHMDE TPQVYLLTDR ILAESDTVDI PLMESFFAEQ LKPNRDADPH KYWEVVDRTT
GEVVDSANWT LDADEDTVHV SGVAAWHEYT VSFLAYIIWD PVEMYNHLTN DWGDKEHEIP
FDIYHPATRK FVFDTFEQWL KDSPQTDVVR FTTFFYQFTL LFDEKRREKV VDWFGCACTV
SPRALDDFEA KYGYRLRPED FVDGGAYNSA WRVPRKAQRD WIDFLSGFVR ENVKQLADMS
HAAGKEAMMF LGDQWIGTEP YKDGFDELGL DAVVGSIGDG TTTRMIADIP GVKYTEGRFL
PYFFPDTFYE GNDPSIEGLD NWRKARRAIL RSPISRMGYG GYLSLAAKFP KFVDTVTHIA
NEFRDIHDRT GGVAAEGELN VAILNSWGKM RSWMAFTVAH ALPNKQTYSY YGILESLSGM
RVNVRFISFD DVLAHGIDSD IDVIINGGPV DTAFTGGDVW TNPKLVETVR AWVRGGGAFV
GVGEPSSAPR FQTGRFFQLA DVIGVDEERY QTLSVDKYFP PVVPDHFITA DVPVDPAARE
AWEQAGYRIP LSGCGGGQSI KPLGGIDFGE PVLNTYPVNE NVTLLRADGG QVQLATNDYG
KGRGVYISGL PYSAANARLL ERVLFYASHN EDKYAAWSSS NPECEVAHFP EQGLYCVINN
TDQPQKTTVT LADGTTEDFD LPDSGIAWRE A
