ID   MELA_LACAC              Reviewed;         732 AA.
AC   G1UB44; F1SVF4; Q5FJ61; Q7WWP9;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   02-SEP-2026, entry version 63.
DE   RecName: Full=Alpha-galactosidase Mel36A {ECO:0000303|PubMed:21827767};
DE            Short=LaMel36A {ECO:0000303|PubMed:21827767};
DE            EC=3.2.1.22 {ECO:0000269|PubMed:21827767, ECO:0000312|EMBL:AAO21867.1, ECO:0000312|EMBL:AAV43263.1};
GN   Name=melA {ECO:0000303|PubMed:16505367, ECO:0000312|EMBL:AAV43263.1};
GN   Synonyms=aga {ECO:0000312|EMBL:AAO21867.1};
GN   OrderedLocusNames=LBA1438 {ECO:0000312|EMBL:AAV43263.1};
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621 {ECO:0000312|Proteomes:UP000006381};
RN   [1] {ECO:0000312|EMBL:AAO21867.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM {ECO:0000303|PubMed:12847288};
RX   PubMed=12847288; DOI=10.1073/pnas.1332765100;
RA   Barrangou R., Altermann E., Hutkins R., Cano R., Klaenhammer T.R.;
RT   "Functional and comparative genomic analyses of an operon involved in
RT   fructooligosaccharide utilization by Lactobacillus acidophilus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8957-8962(2003).
RN   [2] {ECO:0000312|EMBL:AAV43263.1, ECO:0000312|Proteomes:UP000006381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM
RC   {ECO:0000312|Proteomes:UP000006381};
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
RN   [3]
RP   INDUCTION BY RAFFINOSE.
RX   PubMed=16505367; DOI=10.1073/pnas.0511287103;
RA   Barrangou R., Azcarate-Peril M.A., Duong T., Conners S.B., Kelly R.M.,
RA   Klaenhammer T.R.;
RT   "Global analysis of carbohydrate utilization by Lactobacillus acidophilus
RT   using cDNA microarrays.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3816-3821(2006).
RN   [4] {ECO:0007744|PDB:2XN0, ECO:0007744|PDB:2XN1, ECO:0007744|PDB:2XN2}
RP   X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF SUBSTRATE-FREE ENZYME AND IN
RP   COMPLEX WITH ALPHA-GALACTOSE, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, AND
RP   PHYLOGENETIC ANALYSIS.
RX   PubMed=21827767; DOI=10.1016/j.jmb.2011.07.057;
RA   Fredslund F., Hachem M.A., Larsen R.J., Sorensen P.G., Coutinho P.M.,
RA   Lo Leggio L., Svensson B.;
RT   "Crystal structure of alpha-galactosidase from Lactobacillus acidophilus
RT   NCFM: insight into tetramer formation and substrate binding.";
RL   J. Mol. Biol. 412:466-480(2011).
CC   -!- FUNCTION: Hydrolyzes the short-chain alpha-galactosaccharide raffinose.
CC       {ECO:0000305}.
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         Evidence={ECO:0000269|PubMed:21827767};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21827767}.
CC   -!- INDUCTION: By raffinose. {ECO:0000269|PubMed:16505367}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family. {ECO:0000305}.
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DR   EMBL; AY172020; AAO21867.1; -; Genomic_DNA.
DR   EMBL; CP000033; AAV43263.1; -; Genomic_DNA.
DR   RefSeq; WP_003548136.1; NC_006814.3.
DR   PDB; 2XN0; X-ray; 2.50 A; A/B=1-732.
DR   PDB; 2XN1; X-ray; 2.30 A; A/B/C/D=1-732.
DR   PDB; 2XN2; X-ray; 1.58 A; A=1-732.
DR   AlphaFoldDB; G1UB44; -.
DR   SMR; G1UB44; -.
DR   STRING; 272621.LBA1438; -.
DR   CAZy; GH36; Glycoside Hydrolase Family 36.
DR   GeneID; 93289487; -.
DR   KEGG; lac:LBA1438; -.
DR   PATRIC; fig|272621.13.peg.1364; -.
DR   eggNOG; COG3345; Bacteria.
DR   HOGENOM; CLU_009640_2_1_9; -.
DR   OrthoDB; 9758822at2; -.
DR   BioCyc; LACI272621:G1G49-1412-MONOMER; -.
DR   BRENDA; 3.2.1.22; 2846.
DR   EvolutionaryTrace; G1UB44; -.
DR   Proteomes; UP000006381; Chromosome.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IDA:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   GO; GO:1901545; P:response to raffinose; IEP:UniProtKB.
DR   CDD; cd14791; GH36; 1.
DR   FunFam; 3.20.20.70:FF:000118; Alpha-galactosidase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.70.98.60; alpha-galactosidase from lactobacil brevis; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR038417; Alpga-gal_N_sf.
DR   InterPro; IPR050985; Alpha-glycosidase_related.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR   InterPro; IPR002252; Glyco_hydro_36.
DR   InterPro; IPR031705; Glyco_hydro_36_C.
DR   InterPro; IPR031704; Glyco_hydro_36_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   PANTHER; PTHR43053:SF3; ALPHA-GALACTOSIDASE C-RELATED; 1.
DR   PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR   Pfam; PF16874; Glyco_hydro_36C; 1.
DR   Pfam; PF16875; Glyco_hydro_36N; 1.
DR   Pfam; PF02065; Melibiase; 1.
DR   PIRSF; PIRSF005536; Agal; 1.
DR   PRINTS; PR00743; GLHYDRLASE36.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
DR   PDBsum; 2XN0; -.
DR   PDBsum; 2XN1; -.
DR   PDBsum; 2XN2; -.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..732
FT                   /note="Alpha-galactosidase Mel36A"
FT                   /id="PRO_0000439586"
FT   ACT_SITE        482
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:21827767"
FT   ACT_SITE        552
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:21827767"
FT   BINDING         370..371
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:21827767,
FT                   ECO:0007744|PDB:2XN2"
FT   BINDING         415
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:21827767,
FT                   ECO:0007744|PDB:2XN2"
FT   BINDING         447
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:21827767,
FT                   ECO:0007744|PDB:2XN2"
FT   BINDING         480..484
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:21827767,
FT                   ECO:0007744|PDB:2XN2"
FT   BINDING         530..533
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:21827767,
FT                   ECO:0007744|PDB:2XN2"
FT   BINDING         552
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:21827767,
FT                   ECO:0007744|PDB:2XN2"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   TURN            10..13
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          14..18
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          20..29
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          33..41
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           51..53
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          107..116
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          134..143
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   TURN            144..147
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          148..157
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          160..171
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          173..175
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          177..191
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          195..198
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          210..213
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          216..222
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          225..228
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          230..232
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          234..239
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          245..248
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          250..255
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          261..267
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          273..279
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          286..288
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          293..295
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          299..306
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           308..322
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   TURN            327..330
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           332..334
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           340..343
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           349..361
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          366..369
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          371..374
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   TURN            391..393
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           398..407
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          411..416
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          423..425
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           426..430
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           432..434
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           442..445
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          449..452
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           457..471
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          478..481
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           497..502
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           503..521
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          525..529
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           539..542
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          546..549
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           556..566
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   TURN            567..569
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           572..574
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          575..580
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   TURN            585..587
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           593..600
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          603..609
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           611..613
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           616..638
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          639..645
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           647..649
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          651..657
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          663..670
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           677..679
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          691..695
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   TURN            696..698
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   STRAND          701..703
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           704..709
FT                   /evidence="ECO:0007829|PDB:2XN2"
FT   HELIX           714..716
FT                   /evidence="ECO:0007829|PDB:2XN1"
FT   STRAND          718..730
FT                   /evidence="ECO:0007829|PDB:2XN2"
SQ   SEQUENCE   732 AA;  84478 MW;  A712E3D204F89D26 CRC64;
     MTSNLIKFDD QNKVFHLHNK QISYLLSIED GGTLSHLYFG GAVKNYNNQL KYPRLDRGFS
     GNLPESLDRT FSRDSLPKEY SSAGEMDFHT PATIVRNPDG SNALFLAYKS YKIEDGKPDL
     KGLPHSWTKE DDEAQTLIVT LEDKVSKLEY DLLYTIYRDR PVIVRSVQVH NHGEEAVYLE
     KVASMQMDYV DKDFEVITLP GAHANERRVQ RENIGQGIKV FSSYRGTSSH QMNPFMALVD
     HDTNEFMGEA YGFALAYSGN HKFEVERDQF GQIHVNTGIN DYNFKWKLNP NEEFQTPEVL
     MVYSDQGLNK MSQAFHSLIH ERIMRSKFKD QIRPVLVNNW EATYFDFNED KLKTIVDKAK
     KLGLEMFVLD DGWFGHRDDD NSSLGDWKVY KKKFPNGLGH FADYVHEQGL KFGLWFEPEM
     ISYESNLYKE HPDYLMHVPG RKPCPSRNQY VLELGRKEVR DNIFEQMVKI LDSKKIDYIK
     WDMNRSLSDI YESDLPADQQ GEAYHRYVLG YYDLLNKLVT RYPDILFEGC SGGGGRFDVG
     QAYYTPQIWA SDNTDAIERL KIQYGTSLVY PQSMMTSHVS VSPNEQNGRI TPFNTRGAVA
     MWGDLGYELD LTKMSDEESD QVVKQVTEYK KIREVTQFGT LYRLKASASN QCAWMMVDSN
     KNEAVVTVVN VMAHAQPYCT KTKLAGLDPD KRYKNLETDE VFGGDELMHL GFYDPIERGD
     FKAKMYHFKA IN
//