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Entry: A0A3A9K479_9BACI
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ID   A0A3A9K479_9BACI        Unreviewed;       865 AA.
AC   A0A3A9K479;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Arabinanase {ECO:0000313|EMBL:RKL65282.1};
GN   ORFNames=CR203_21670 {ECO:0000313|EMBL:RKL65282.1};
OS   Salipaludibacillus neizhouensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX   NCBI_TaxID=885475 {ECO:0000313|EMBL:RKL65282.1, ECO:0000313|Proteomes:UP000281498};
RN   [1] {ECO:0000313|EMBL:RKL65282.1, ECO:0000313|Proteomes:UP000281498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 13187 {ECO:0000313|EMBL:RKL65282.1,
RC   ECO:0000313|Proteomes:UP000281498};
RA   Wang H.;
RT   "Bacillus sp. nov., a halophilic bacterium isolated from a Keqin Lake.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
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:RKL65282.1}.
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DR   EMBL; PDOE01000019; RKL65282.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A9K479; -.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000281498; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.40.128.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR046780; aBig_2.
DR   InterPro; IPR032291; Abn2_C.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR006558; LamG-like.
DR   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR   Pfam; PF20578; aBig_2; 1.
DR   Pfam; PF16369; GH43_C; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   SMART; SM00560; LamGL; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281498};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..865
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017226571"
FT   DOMAIN          726..857
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   REGION          30..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        62
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        311
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            245
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   865 AA;  95403 MW;  E5A641C7B5936E1B CRC64;
     MRKTSAQRIT FIVLILLLMI PLTVSANGKS GEPNVPPNEN NNKPHLDYQG DSMDFENASV
     HDPSIIKADG MYYVFGTHIA AAKSEDLINW TNFTNGYTRT DNTLYGDLSE NLSGSFEWAG
     ENDADSRGGF GVWAPDIFWN EDYVNEDGTK GTYMIYYSVS STWQRSAIGY AVSKDIEGPY
     EYVDTIVYSG FTKVEAYDNN SDVNKQWENT NISGLIEDGV FAEPNPEWFQ SDDVYNTRLY
     PNAIDANMFY DEDGTLWMTY GSWSGGIYMY ELDKSTGQPI YPGEDGTTED GRIIDRYFGT
     QIAGGFGHSI EGPYAYYDDE LDYYYLYLTY GGLAATGGYQ MRVFRSESPT GPYVDAAGEP
     AALPDSLDDG TVGNKVNSYA HSDFGNKLMG NFLFERKIGD PGSGVGHTYA APGHNSVHYD
     QETGERFVVF HTRFPNRGES HEVRVHQLFM NKEGWPVATP FRYSGETLDK VNKQDIVGEY
     KFVNHGKEIT GSVTNSVFVT LNKDNTVSGD VTGTWKKTGH NKAELTIDGK TYDGVFLRQY
     DTSSELTVMT FTAMSNEGVA VWGTKTLDRT DEEVIEAVVN DLDFGDLDSV ISNLTLPTEG
     TQNTVISWET SDPGVVTDTG EVTRPAVGEE DATATLTATI TKDGTTITKT FDITVLAYLP
     AGLTAHYAFE STLEDSTENF GTGTMTGNRI NNTGGMITYT DGVRGEAAVF NGDSGVRLPD
     GLISSHTYSV SLWLKPESLS AYTTAFFGAR SDSSWISLLP GGNGNGQTMV WSGSQRWVDS
     TTSRTIPIDQ WSHVVFTVDE GNIKVYIDGV LQHDGNNFPN IFTTTNGNFS LAVNWWDTPF
     KGLMDELRVY EGALSPEEIV ELAQK
//
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