ID A0A0U3APB2_9ALTE Unreviewed; 1191 AA.
AC A0A0U3APB2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:ALS99762.1};
GN ORFNames=AT746_16805 {ECO:0000313|EMBL:ALS99762.1};
OS Lacimicrobium alkaliphilum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Lacimicrobium.
OX NCBI_TaxID=1526571 {ECO:0000313|EMBL:ALS99762.1, ECO:0000313|Proteomes:UP000068447};
RN [1] {ECO:0000313|EMBL:ALS99762.1, ECO:0000313|Proteomes:UP000068447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YelD216 {ECO:0000313|EMBL:ALS99762.1,
RC ECO:0000313|Proteomes:UP000068447};
RA Kim S.-G., Lee Y.-J.;
RT "Complete genome of Lacimicrobium alkaliphilum KCTC 32984.";
RL Submitted (DEC-2015) 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}.
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DR EMBL; CP013650; ALS99762.1; -; Genomic_DNA.
DR RefSeq; WP_062482755.1; NZ_CP013650.1.
DR AlphaFoldDB; A0A0U3APB2; -.
DR STRING; 1526571.AT746_16805; -.
DR KEGG; lal:AT746_16805; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000068447; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18832; GH43_GsAbnA-like; 1.
DR Gene3D; 2.40.128.10; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
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 PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF20578; aBig_2; 2.
DR Pfam; PF16369; GH43_C; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF13385; Laminin_G_3; 2.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ALS99762.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068447};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1191
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006836106"
FT DOMAIN 484..589
FT /note="Extracellular endo-alpha-(1->5)-L-arabinanase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16369"
FT DOMAIN 615..681
FT /note="Atrophied bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF20578"
FT DOMAIN 907..977
FT /note="Atrophied bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF20578"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 347
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 294
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 1191 AA; 128976 MW; DC621CBAFC0A9450 CRC64;
MHGSICKLTQ KYSLPGLARM LAIASLGFCG NAFAGWQTVE SATVEQENRV YVRGQGYYTD
NSIHSGDEPL EGEAYRVVIT QSTHTVTNAS GTNEQGHPYF EVADLSEIIR VWFANGRGSF
GYSAELQQET SGSMPELSEP PVYNNATVHD PSVVQDENGT FYVFGSHLAV ARSEDLMSWE
LIATDVTDDN PLFDTYATEA AEGIAWSGGT IGSWAADVIR LADGKYYFYY NHCASPDTGL
CDASRSYLGV AVSDDVEGPY QDRGLILRSG HVGDENPGID GNPYNGNIHP NAIDPDVFFD
KEGRLWMVYG SYSGGIWIME MDPQSGFPLE GQGYGTKLMG GYYSAIEGPY MLYSPESDYY
YLFTSFGGYE QNDGYNMRIA RSRNPDGPFV DAQGLDMIGA SGGWGSIEPY GVKLMGGHLF
KARPGDPGTD HGYMAPGHNS AYYDEQSGRH FVIFHTRFPE GGEGHQIRVH ELFVNADGWL
VASPHRYAPI EGENVVSEND ALGVYQFINH EKDINREAKV SSYLALEAEG QIGGDFSGSY
VLGHDNELVL NIDGLGSFDG VLLWQWNDNI QQLVPSFSAI DTDGQSVWGS RLPPADTQET
LSNIGSSLTL PEASISDLEL PTLGSRGASI TWQSDNTDVI STDGRVTRPN TGEPDATVTL
SATVELDGQL LTKEFTVTVE ARKPFNRIAR YSFEQDLSDN AGYQADGSVT GTTPDTTDGQ
IDYASGQFGD ALWLNGSSGV RLPDGLIDNN AYTVSLWLNP TQLTQFTPAF FGAATPENWL
SLVPWSWDGN TMLWSGSQVW YDATTGEQIP ADSWSHVAFA VDNGNIRVYI DGEQKFSGNN
FADLFSGQSA VFTLGVNYWD IPFNGLIDEL SLYEGALSAE EIRALDIDRL PTDQLLQSAV
SLLDLGELDS VRQDLSLPQT GAYASVIEWQ SSNPAVLSAS GEVNRPASHE QDAIVTLTAT
LTLDGFQASR EFQVTVRSLA PPAPVAEFNF DVNDLSEAGG NFAPGQSTGP RLDQAGGNLS
FTPGVTGSAL QLDGNSGVKL PDNLIIGSQY SFALWLNPSQ LTQFTPALFA AASPDSWVSL
VPNGVPAVNG DTMLWSGTNW YDAGMGTQIP VGSWSHIAVV ANNGALQIFL NGQQVFSGNG
FPDVFASPGN EFGLGVNFWD TPYQGLLDEV RFYAEAITAD EVQQLYLSSQ P
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