ID X2GC52_9THEO Unreviewed; 458 AA.
AC X2GC52;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Endo-1,5-arabinanase {ECO:0000313|EMBL:AHN16715.1};
DE EC=3.2.1.99 {ECO:0000313|EMBL:AHN16715.1};
GN Name=abn43A {ECO:0000313|EMBL:AHN16715.1};
OS Caldanaerobius polysaccharolyticus.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobius.
OX NCBI_TaxID=44256 {ECO:0000313|EMBL:AHN16715.1};
RN [1] {ECO:0000313|EMBL:AHN16715.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KMCJ {ECO:0000313|EMBL:AHN16715.1};
RA Han Y., Abdel-Hemid A., Meyer B., Dodd D., Mackie R.I., Cann I.;
RT "Molecular analysis of an alpha-L-arabinofuranosidase and an endo-1,5-
RT arabinanase from the thermophilic bacterium, Caldanaerobius
RT polysaccharolyticus.";
RL Submitted (DEC-2013) 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, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; KJ009331; AHN16715.1; -; Genomic_DNA.
DR AlphaFoldDB; X2GC52; -.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd08998; GH43_Arb43a-like; 1.
DR Gene3D; 2.40.128.10; -; 1.
DR InterPro; IPR032291; Abn2_C.
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; PF16369; GH43_C; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:AHN16715.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:AHN16715.1}.
FT DOMAIN 341..453
FT /note="Extracellular endo-alpha-(1->5)-L-arabinanase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16369"
FT ACT_SITE 48
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 168
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 458 AA; 52069 MW; BCE97CD9EE5CA1E6 CRC64;
MLGIIMSSCS NDNGGSSIIY PKEPPKDRLY DSSIINDEAK WGTMNAHDPS IFKDGEWYYI
FSTDVKVGGM PRAGIQVRKS KDLIHWQWVG YALDGVPEEA EKWTGATNLW APDVTKIGDT
YYLYYVASTF GKNQSFIGVA TSKSIEGPWE DKGAVLKSRQ GDEWNALDPN IVYDADGNMW
MDFGSFFGGI YIIQLDPKTG KPLEGAKPKL IARRGGQDAI EGPYIIYNKQ QKKYYLFTSF
DSLMYDYNVR VARSDRIDGP YVDYNGNLMT DTSLNAGTKI LNSYQFEGSN GWVATGHNSV
LQDGNDYYII HHARGDQDTN WPYLHVRKIL WSDDGWPMVS PERYAGEFEQ QLNREDVIGD
WQIIELDKDD NSQLTSTTIT LLKNGKIDKG NGKDYWEFSG KNNVKLYFYD PDHALKGAYR
IETAKVIPAW DWENWRPTLV FTGFEQNGTA VWGKKIKP
//
