GH109_ELIME
ID GH109_ELIME Reviewed; 444 AA.
AC A4Q8F7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Alpha-N-acetylgalactosaminidase;
DE EC=3.2.1.49;
DE AltName: Full=Glycosyl hydrolase family 109 protein;
GN Name=nagA;
OS Elizabethkingia meningoseptica (Chryseobacterium meningosepticum).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, BIOTECHNOLOGY, AND X-RAY
RP CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RC STRAIN=ATCC 33958;
RX PubMed=17401360; DOI=10.1038/nbt1298;
RA Liu Q.P., Sulzenbacher G., Yuan H., Bennett E.P., Pietz G., Saunders K.,
RA Spence J., Nudelman E., Levery S.B., White T., Neveu J.M., Lane W.S.,
RA Bourne Y., Olsson M.L., Henrissat B., Clausen H.;
RT "Bacterial glycosidases for the production of universal red blood cells.";
RL Nat. Biotechnol. 25:454-464(2007).
CC -!- FUNCTION: Glycosidase that has specific alpha-N-acetylgalactosaminidase
CC activity. {ECO:0000269|PubMed:17401360}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine
CC residues from human blood group A and AB mucin glycoproteins,
CC Forssman hapten and blood group A lacto series glycolipids.;
CC EC=3.2.1.49; Evidence={ECO:0000269|PubMed:17401360};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:17401360};
CC Note=Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
CC {ECO:0000269|PubMed:17401360};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25.1 mM for Galalpha-pNP {ECO:0000269|PubMed:17401360};
CC KM=3.6 mM for Galbeta-pNP {ECO:0000269|PubMed:17401360};
CC KM=0.077 mM for GalNAcalpha-pNP {ECO:0000269|PubMed:17401360};
CC KM=0.23 mM for GalNAcbeta-pNP {ECO:0000269|PubMed:17401360};
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:17401360};
CC -!- BIOTECHNOLOGY: Specifically cleaves the blood group A antigen at
CC neutral pH with low consumption of recombinant enzyme. It is therefore
CC a good candidate to participate in the development of universal red
CC blood cells by removing blood group A antigen.
CC {ECO:0000269|PubMed:17401360}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The juice of life - Issue 98
CC of October 2008;
CC URL="https://web.expasy.org/spotlight/back_issues/098";
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DR EMBL; AM039444; CAJ01376.1; -; Genomic_DNA.
DR PDB; 2IXA; X-ray; 2.30 A; A=1-444.
DR PDB; 2IXB; X-ray; 2.40 A; A=1-444.
DR PDBsum; 2IXA; -.
DR PDBsum; 2IXB; -.
DR AlphaFoldDB; A4Q8F7; -.
DR SMR; A4Q8F7; -.
DR STRING; 1216967.L100_15585; -.
DR CAZy; GH109; Glycoside Hydrolase Family 109.
DR PRIDE; A4Q8F7; -.
DR eggNOG; COG0673; Bacteria.
DR BRENDA; 3.2.1.49; 1374.
DR EvolutionaryTrace; A4Q8F7; -.
DR GO; GO:0008456; F:alpha-N-acetylgalactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; NAD.
FT CHAIN 1..444
FT /note="Alpha-N-acetylgalactosaminidase"
FT /id="PRO_0000348545"
FT BINDING 30..31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 101..104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 121..122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 179
FT /ligand="substrate"
FT BINDING 208..212
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 213
FT /ligand="substrate"
FT BINDING 225..228
FT /ligand="substrate"
FT BINDING 225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 307
FT /ligand="substrate"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2IXA"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:2IXA"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:2IXA"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:2IXA"
FT TURN 336..341
FT /evidence="ECO:0007829|PDB:2IXA"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 349..354
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 375..389
FT /evidence="ECO:0007829|PDB:2IXA"
FT HELIX 397..415
FT /evidence="ECO:0007829|PDB:2IXA"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:2IXA"
FT TURN 426..433
FT /evidence="ECO:0007829|PDB:2IXA"
SQ SEQUENCE 444 AA; 50211 MW; 31457EDBC89518FB CRC64;
MGALIPSSTL FNIFDFNPKK VRIAFIAVGL RGQTHVENMA RRDDVEIVAF ADPDPYMVGR
AQEILKKNGK KPAKVFGNGN DDYKNMLKDK NIDAVFVSSP WEWHHEHGVA AMKAGKIVGM
EVSGAITLEE CWDYVKVSEQ TGVPLMALEN VCYRRDVMAI LNMVRKGMFG ELVHGTGGYQ
HDLRPVLFNS GINGKNGDGV EFGEKAFSEA KWRTNHYKNR NGELYPTHGV GPLHTMMDIN
RGNRLLRLSS FASKARGLHK YIVDKGGESH PNAKVEWKQG DIVTTQIQCH NGETIVLTHD
TSLQRPYNLG FKVQGTEGLW EDFGWGEAAQ GFIYFEKIMN HSHRWDSSEK WIKEYDHPMW
KKHEQKAVGA GHGGMDYFLD NTFVECIKRN EAFPLDVYDL ATWYSITPLS EKSIAENGAV
QEIPDFTNGK WKNAKNTFAI NDDY
