ID GLAA_AKKM8 Reviewed; 596 AA.
AC B2UL12;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Alpha-1,3-galactosidase A;
DE EC=3.2.1.n1;
DE AltName: Full=Exo-alpha-galactosidase A;
DE EC=3.2.1.22;
DE Flags: Precursor;
GN Name=glaA; OrderedLocusNames=Amuc_1463;
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP
RC 107961 / Muc;
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
CC -!- FUNCTION: Alpha-galactosidase that specifically removes branched alpha-
CC 1,3-linked galactose residues present in blood group B antigens. Has no
CC activity toward linear alpha-1,3-linked galactose residues (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-
CC galactosidic residues, producing free D-galactose.; EC=3.2.1.n1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 110 family. A subfamily.
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; CP001071; ACD05285.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UL12; -.
DR SMR; B2UL12; -.
DR STRING; 349741.Amuc_1463; -.
DR CAZy; GH110; Glycoside Hydrolase Family 110.
DR PaxDb; 349741-Amuc_1463; -.
DR KEGG; amu:Amuc_1463; -.
DR eggNOG; COG5434; Bacteria.
DR HOGENOM; CLU_017693_0_0_0; -.
DR Proteomes; UP000001031; Chromosome.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 3.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF13229; Beta_helix; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..596
FT /note="Alpha-1,3-galactosidase A"
FT /id="PRO_5000370228"
FT REPEAT 351..373
FT /note="PbH1 1"
FT REPEAT 482..504
FT /note="PbH1 2"
FT REPEAT 515..537
FT /note="PbH1 3"
FT REPEAT 547..569
FT /note="PbH1 4"
FT REGION 23..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 65952 MW; FF5E844064C2FADD CRC64;
MQNPVASLLF ILAMLTGPCP AADYPERTER TQSAGNHVWH IDPDKGNDGN PGTAPSTAWK
SMAPANRLIM ARGDTLVIHP GEHAVSLALM GEGSKQAPVT IRFMPGRHIF KHGALMTGKP
QISNTNDAPN EPKAMAIRLM EAKNIRLEGK PGATDILLEG KAIFVCMEHA ENVSLNGLGF
DYLHPTMGEF LVTEVEGDTM KATIPDGTLY TVKDGNLTWH GPGWEFRMGG YSKVFDSASG
TFQGRFDPGK TVIRELSPGK ISITFKEGSP TMKPGQSYQN RNTRRDCCGF FQYRSKNILW
NNCHIYYMHG MGVVSQFCEN IMFSHLKIAP RPRSLRTNSS WADNLHFSGC RGKIIVKDCV
LGASHDDAVN VHGTHLRIID RPAPNKITVR FMHPQTFGFD AFAAGDRIDY VSCNTLVPYA
SNTVSGVKQL NEKEIELTLQ HPNPGNIQPD DVVENVTWTP SVHISNTVCR HIPTRGFLLT
TRKPVLVERC RFEKTGMPAI LVEDDASGWY ESGVVRNMTI SRNTFIQCGE AVIQIVPHAP
RPEGDVHRNI TITGNTFDLK NGTAIRIRHT GDVKAEKNTF TKDGKKIPEE KAVDIR
//
