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Database: UniProt
Entry: A0A1X2H8G7_SYNRA
LinkDB: A0A1X2H8G7_SYNRA
Original site: A0A1X2H8G7_SYNRA 
ID   A0A1X2H8G7_SYNRA        Unreviewed;       956 AA.
AC   A0A1X2H8G7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=BCR43DRAFT_441888 {ECO:0000313|EMBL:ORY94808.1};
OS   Syncephalastrum racemosum (Filamentous fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX   NCBI_TaxID=13706 {ECO:0000313|EMBL:ORY94808.1, ECO:0000313|Proteomes:UP000242180};
RN   [1] {ECO:0000313|EMBL:ORY94808.1, ECO:0000313|Proteomes:UP000242180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2496 {ECO:0000313|EMBL:ORY94808.1,
RC   ECO:0000313|Proteomes:UP000242180};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00001412};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORY94808.1}.
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DR   EMBL; MCGN01000007; ORY94808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2H8G7; -.
DR   STRING; 13706.A0A1X2H8G7; -.
DR   InParanoid; A0A1X2H8G7; -.
DR   OMA; QTEFPVP; -.
DR   OrthoDB; 1032627at2759; -.
DR   Proteomes; UP000242180; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR   Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF13364; BetaGal_ABD2; 2.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ORY94808.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242180};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..956
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012959346"
FT   DOMAIN          390..539
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000259|SMART:SM01029"
SQ   SEQUENCE   956 AA;  106644 MW;  248CA8E54626CAD4 CRC64;
     MALAKCVFTS ITAAIMATAV LAIPAPLQFD KRDSFDKPVT WDNHTLMING ERLFLYSGEF
     HYYRLPSPGL WVDIMEKFKA LDFNGVSFYF YWGYHSPKKG IYDFSGVRDV QKAIDAATQA
     DLEIITRPGP YINAEVDGGG FPGWTKTQRA VARKNSTENN ENWSEWLSAI DAKIVPNQIT
     HGGRVILNQI DNEYAANTDE YYMEAIKEQF LKDGMDVPTI FNDPNTGAHF VHGIGAPDIY
     GWDSYPAGFD CSNPDVWPNN ANFGWYDYHM ANNPDQPVAL YEFQGGAFDP WGGPGYDACR
     KMVSERYAKV YYKNNYANGA RIQNLYMGYG TSWGGIAIPS VYTSYDYGAP ISEPGLMTPK
     AHEVRLQGME ALSCIPSSLS CLPTDSMPQW IMMTSILMAG SIKRQARRST FKAAGKTINI
     PRSSKLVLNG RDAKMLVADY AFNSQELAYT TSEIFTHQSM GSFDVLLVYA YEKEEGEFAL
     KTSKNAQVQS KHKSVKSKYT NGLLQVNYRH PKGTTPISIQ QDTTDLLVLV AGYDSATKWW
     APIVDKDSQQ RVLVHGPYLV RSARIQGSTL SLRADIDETT DIQIVAPDSV TQFEWNGKAV
     ELTKSKEGIW QGKLKFTQPK VEYTDLSKAK WQYQQGSPES EPDFDDSDWI KADHLETNSI
     TPHVTYPVLF ADDYGFHTGS LWFRGTFNGS DAITGFNLTA NTGTASAWVA WLNGKYLGGF
     ESGNQAFTDL GDTLKSDGEN VISLLVWTVG NADDWNANDA YKEARGFTMA QLLGVSNQTI
     WSIDWKVQGN LGGEDLADPV RGPYNEGGLY GERKGWHLPD FETDDAWKTA SVPESKNRSG
     VSWYRTEFEV NVPEGYDVPM GLRFKDKTDH RYRALVFLNG WQLGRYANDL GPQELYYLPE
     GILNTSGKNT LALAVIPLDE AAQVGEVVLE PYGVLQSAKP KVDLVESPGY DKSKRG
//
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