BGAL_HALLT
ID BGAL_HALLT Reviewed; 700 AA.
AC B9LW38;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Beta-galactosidase Bga;
DE Short=Beta-gal;
DE EC=3.2.1.23;
GN OrderedLocusNames=Hlac_2868;
OS Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS 34).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=416348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA Woese C.R., Kyrpides N.C.;
RT "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT strain ACAM 34.";
RL Stand. Genomic Sci. 11:70-70(2016).
RN [2]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX PubMed=23320757; DOI=10.1186/1472-6750-13-3;
RA Karan R., Capes M.D., DasSarma P., DasSarma S.;
RT "Cloning, overexpression, purification, and characterization of a
RT polyextremophilic beta-galactosidase from the Antarctic haloarchaeon
RT Halorubrum lacusprofundi.";
RL BMC Biotechnol. 13:3-3(2013).
CC -!- FUNCTION: Cleaves o-nitrophenyl-beta-D-galactopyranoside (ONPG) in
CC vitro. {ECO:0000269|PubMed:23320757}.
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 -!- ACTIVITY REGULATION: Requires 4 M NaCl or KCl for maximal activity.
CC {ECO:0000269|PubMed:23320757}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5 with ONPG as substrate. Measured at 37 degrees
CC Celsius and in 4 M KCl. {ECO:0000269|PubMed:23320757};
CC Temperature dependence:
CC Optimum temperature is around 50-55 degrees Celsius in 4 M KCl and at
CC pH 6.5. Partial activity (10-13% of maximum) at temperatures from 4-
CC 10 degrees Celsius. {ECO:0000269|PubMed:23320757};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000305}.
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DR EMBL; CP001366; ACM58428.1; -; Genomic_DNA.
DR RefSeq; WP_012659244.1; NC_012028.1.
DR PDB; 6LVW; X-ray; 2.49 A; A=1-700.
DR PDBsum; 6LVW; -.
DR AlphaFoldDB; B9LW38; -.
DR SMR; B9LW38; -.
DR STRING; 416348.Hlac_2868; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR EnsemblBacteria; ACM58428; ACM58428; Hlac_2868.
DR GeneID; 7399104; -.
DR KEGG; hla:Hlac_2868; -.
DR eggNOG; arCOG04085; Archaea.
DR HOGENOM; CLU_012430_1_0_2; -.
DR OMA; SRRHYCF; -.
DR BRENDA; 3.2.1.23; 11918.
DR Proteomes; UP000000740; Chromosome 2.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR013738; Beta_galactosidase_Trimer.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR003476; Glyco_hydro_42.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; PTHR36447; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR PIRSF; PIRSF001084; B-galactosidase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..700
FT /note="Beta-galactosidase Bga"
FT /id="PRO_0000428831"
FT REGION 648..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 312
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 360..363
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6LVW"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6LVW"
FT TURN 143..147
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 205..233
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 290..301
FT /evidence="ECO:0007829|PDB:6LVW"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 331..342
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:6LVW"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 375..389
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 406..414
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 423..435
FT /evidence="ECO:0007829|PDB:6LVW"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 466..478
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 509..519
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 546..560
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:6LVW"
FT TURN 571..574
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 578..582
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 584..591
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:6LVW"
FT HELIX 597..610
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 623..628
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 631..636
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:6LVW"
FT STRAND 687..689
FT /evidence="ECO:0007829|PDB:6LVW"
SQ SEQUENCE 700 AA; 78057 MW; 017F53E9EF975953 CRC64;
MRLGVCYFPE HWPSEEWERD VAAMADAGLE YVRMAEFSWG VLEPERGTFD FEWLDEAIEL
IGDHGMQAVL CTPTATPPKW LVDERPSIRQ EDPDGTVREH GSRRHYCFNS DAYREETARI
VERVTERYAD SPHVAGWQTD NEFGCHETVR CYCDDCADAF RTWLADRYGD IDRLNEAWGN
AFWSQQYGSF DEIDPPGPTP AEHHPSRLLA YARFSSDSVV EYNRLHADLI READPDWFVT
HNFMGRFPTL NAYDVSEDLD RVAWDSYPTG FVQDRYDGEA SPDQLRAGDP DQVGMDHDIY
RSALDRPFWV MEQQPGDVNW PPHCPQPGEG AMRLWAHHAA AHGADAVLYF RWRRCLEGQE
QYHAGLRKAD GSPDRGYADA AHTSEEFATL DGASHVDAPV AVVFDYDSLW ALNAQPHAPD
FDYWALQEAF YGAVRGRGVQ VDVVPPSADL SGYAAVVAPA LHLVTEDLAD RLTDYIAGGG
EVLFGPRTGV KDAENKLRPM SQPGPLTDLV GATVDQHESL PRRLETTVRR VGDPTDDSEE
IAAPPVSFRT WAEWLDPDAA EPQYAYDVDG PADGRPAVVT NTVGDGQVTY CGVWPESDLA
DALASDLLDR AGVRYAERLP DGVRIGYRGG RTWVTNFTSD RLRLPEIDPE SLAVDDTDRD
GFDPMADDDK DSSADGIVVG PYGVAVIEGD CVDGLRIAQT
