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Database: UniProt
Entry: F5ZFA5_ALTNA
LinkDB: F5ZFA5_ALTNA
Original site: F5ZFA5_ALTNA 
ID   F5ZFA5_ALTNA            Unreviewed;       714 AA.
AC   F5ZFA5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
DE            EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
GN   OrderedLocusNames=ambt_17295 {ECO:0000313|EMBL:AEF04961.1};
OS   Alteromonas naphthalenivorans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=715451 {ECO:0000313|EMBL:AEF04961.1, ECO:0000313|Proteomes:UP000000683};
RN   [1] {ECO:0000313|EMBL:AEF04961.1, ECO:0000313|Proteomes:UP000000683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17741 / KACC 18427 / KCTC 11700BP / SN2
RC   {ECO:0000313|Proteomes:UP000000683};
RX   PubMed=21705606; DOI=10.1128/JB.05252-11;
RA   Jin H.M., Jeong H., Moon E.J., Math R.K., Lee K., Kim H.J., Jeon C.O.,
RA   Oh T.K., Kim J.F.;
RT   "Complete genome sequence of the polycyclic aromatic hydrocarbon-degrading
RT   bacterium Alteromonas sp. strain SN2.";
RL   J. Bacteriol. 193:4292-4293(2011).
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:0000256|ARBA:ARBA00001255,
CC         ECO:0000256|PIRNR:PIRNR005536};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase.
CC       {ECO:0000256|PIRNR:PIRNR005536}.
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DR   EMBL; CP002339; AEF04961.1; -; Genomic_DNA.
DR   RefSeq; WP_013785880.1; NC_015554.1.
DR   AlphaFoldDB; F5ZFA5; -.
DR   KEGG; alt:ambt_17295; -.
DR   eggNOG; COG3345; Bacteria.
DR   HOGENOM; CLU_009640_3_1_6; -.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000000683; Chromosome.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   CDD; cd14791; GH36; 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; 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   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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR005536};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005536}.
FT   DOMAIN          25..245
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          623..700
FT                   /note="Glycosyl hydrolase family 36 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16874"
FT   ACT_SITE        455
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        520
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
SQ   SEQUENCE   714 AA;  79582 MW;  207632AB6CEC3816 CRC64;
     MSSLTAFVRL DNAKTTLIFD CQGRMPTLIY YGQQLKTATT PDMLALLNTR QEAKCAPVIE
     PPISLVPTHG EGVTGSPGLE ISGDADQWSA GFTLSDIEQT DTSLTFTAVD ADRQMQLITR
     VVLDAETTVA TFTSSIENQG ESTLQLNYLN AASLALPTTM SKIKSFEGRW SNEFQTADHD
     LFFGSYVREN RRGKTSHDTF PGLIAFANGT GELVGECFGF HLGASANHKF RAEMMADGRS
     YVQFGELLFP GEVTLGAGES YTSPVLYAGF GDAGFSSLSQ QFHNFIRNNV LTHSADITSA
     QHKPRPVHYN TWEGIYFDHD EATLKALADK VAPLGIERFV LDGGWFKGRR NDKAGLGDWT
     VDEAIYPEGL DGLIDHVTDK GMEFGIWFEP EMVNPDSDLY RAHPEWALHT KNNPHVPFRN
     QYVLDLTNPE VVEYLYKVIT DVLSTYPKIS YIKWDMNRDV NHPGNLHGKP AMNGQMAALY
     TLIDRVKAAH PGIEIESCCS GGGRVDLGIL PHTDRFWTSD SNDALDRLYI QRGFSYFFPS
     EVMGAHVGPR DCHITGRNLP IEIRSAVSMF GHMGIEMDPR ELTEHEQDTL KSAISLYKKY
     RHITHGGDLY RMDDDGLNVK FGYVSKDKAE GIFAYNSVKE TGRTTPSRFY FAGLDADKSY
     TLERVWPGTL KEYSPSILQK TDGQVFSGEA LMKYGMQMPV LFPQTSLIYT AKEV
//
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