MELA_LACAC
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 03-AUG-2022, entry version 50.
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; Firmicutes; 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 {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 RefSeq; YP_194294.1; 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 PDBsum; 2XN0; -.
DR PDBsum; 2XN1; -.
DR PDBsum; 2XN2; -.
DR AlphaFoldDB; G1UB44; -.
DR SMR; G1UB44; -.
DR STRING; 272621.LBA1438; -.
DR CAZy; GH36; Glycoside Hydrolase Family 36.
DR PRIDE; G1UB44; -.
DR EnsemblBacteria; AAV43263; AAV43263; LBA1438.
DR GeneID; 56943018; -.
DR KEGG; lac:LBA1438; -.
DR PATRIC; fig|272621.13.peg.1364; -.
DR eggNOG; COG3345; Bacteria.
DR HOGENOM; CLU_009640_2_1_9; -.
DR OMA; WEGIYFD; -.
DR BioCyc; LACI272621:G1G49-1412-MON; -.
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:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
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 Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 2.70.98.60; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR038417; Alpga-gal_N_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 InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF16874; Glyco_hydro_36C; 1.
DR Pfam; PF16875; Glyco_hydro_36N; 1.
DR PIRSF; PIRSF005536; Agal; 1.
DR PRINTS; PR00743; GLHYDRLASE36.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
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 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 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 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 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 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 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 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
