ID B3EYN2_GEOSE Unreviewed; 848 AA.
AC B3EYN2;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Extracellular arabinanase {ECO:0000313|EMBL:ACE73680.1};
DE SubName: Full=Family 43 glycosylhydrolase {ECO:0000313|EMBL:QOR82950.1};
GN Name=abnA {ECO:0000313|EMBL:ACE73680.1};
GN ORFNames=IMZ17_09865 {ECO:0000313|EMBL:QOR82950.1};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422 {ECO:0000313|EMBL:ACE73680.1};
RN [1] {ECO:0000313|EMBL:ACE73680.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T-6 {ECO:0000313|EMBL:ACE73680.1};
RX PubMed=8031084;
RA Gat O., Lapidot A., Alchanati I., Regueros C., Shoham Y.;
RT "Cloning and DNA sequence of the gene coding for Bacillus
RT stearothermophilus T-6 xylanase.";
RL Appl. Environ. Microbiol. 60:1889-1896(1994).
RN [2] {ECO:0000313|EMBL:ACE73680.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T-6 {ECO:0000313|EMBL:ACE73680.1};
RX PubMed=10368143;
RA Shulami S., Gat O., Sonenshein A.L., Shoham Y.;
RT "The glucuronic acid utilization gene cluster from Bacillus
RT stearothermophilus T-6.";
RL J. Bacteriol. 181:3695-3704(1999).
RN [3] {ECO:0000313|EMBL:ACE73680.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T-6 {ECO:0000313|EMBL:ACE73680.1};
RX PubMed=11358519; DOI=10.1046/j.1432-1327.2001.02193.x;
RA Zaide G., Shallom D., Shulami S., Zolotnitsky G., Golan G., Baasov T.,
RA Shoham G., Shoham Y.;
RT "Biochemical characterization and identification of catalytic residues in
RT alpha-glucuronidase from Bacillus stearothermophilus T-6.";
RL Eur. J. Biochem. 268:3006-3016(2001).
RN [4] {ECO:0000313|EMBL:ACE73680.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T-6 {ECO:0000313|EMBL:ACE73680.1};
RX PubMed=11322943; DOI=10.1016/S0014-5793(01)02360-2;
RA Bravman T., Zolotnitsky G., Shulami S., Belakhov V., Solomon D., Baasov T.,
RA Shoham G., Shoham Y.;
RT "Stereochemistry of family 52 glycosyl hydrolases: a beta-xylosidase from
RT Bacillus stearothermophilus T-6 is a retaining enzyme.";
RL FEBS Lett. 495:39-43(2001).
RN [5] {ECO:0000313|EMBL:ACE73680.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T-6 {ECO:0000313|EMBL:ACE73680.1};
RX PubMed=17142383; DOI=10.1128/AEM.02367-06;
RA Shulami S., Zaide G., Zolotnitsky G., Langut Y., Feld G., Sonenshein A.L.,
RA Shoham Y.;
RT "A two-component system regulates the expression of an ABC transporter for
RT xylo-oligosaccharides in Geobacillus stearothermophilus.";
RL Appl. Environ. Microbiol. 73:874-884(2007).
RN [6] {ECO:0000313|EMBL:ACE73680.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T-6 {ECO:0000313|EMBL:ACE73680.1};
RA Shoham Y., Shulami S., Ben-David A., Langut Y.;
RT "Hemicellulose utilization cluster in Geobacillus stearothermophilus strain
RT T-6.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0007829|PDB:5HO0}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RA Lansky S., Shwartstien S., Salama R., Shoham Y., Shoham G.;
RT "Crystal structure of AbnA (closed conformation), a GH43 extracellular
RT arabinanase from Geobacillus stearothermophilus.";
RL Submitted (JAN-2016) to the PDB data bank.
RN [8] {ECO:0007829|PDB:5HO2}
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RA Lansky S., Shwartstien O., Salama R., Shoham Y., Shoham G.;
RT "Crystal structure of AbnA (open conformation), a GH43 extracellular
RT arabinanase from Geobacillus stearothermophilus.";
RL Submitted (JAN-2016) to the PDB data bank.
RN [9] {ECO:0007829|PDB:5HOF}
RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RA Lansky S., Shwartstien O., Salama R., Shoham Y., Shoham G.;
RT "Crystal structure of AbnA, a GH43 extracellular arabinanase from
RT Geobacillus stearothermophilus, in complex with arabinopentaose.";
RL Submitted (JAN-2016) to the PDB data bank.
RN [10] {ECO:0007829|PDB:5HP6}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RA Lansky S., Salama R., Shwartstien O., Shoham Y., Shoham G.;
RT "Structure of AbnA, a GH43 extracellular arabinanase from Geobacillus
RT stearothermophilus (a new conformational state).";
RL Submitted (JAN-2016) to the PDB data bank.
RN [11] {ECO:0007829|PDB:5HON}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 640-848 IN COMPLEX WITH CALCIUM.
RA Lansky S., Azoulai D., Shwartstien O., Shoham Y., Shoham G.;
RT "Structure of Domain 4 of AbnA, a GH43 extracellular arabinanase from
RT Geobacillus stearothermophilus, in complex with arabinotriose.";
RL Submitted (JAN-2016) to the PDB data bank.
RN [12] {ECO:0007829|PDB:5HO9}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-639.
RA Lansky S., Salama R., Shwartstien O., Shoham Y., Shoham G.;
RT "Structure of truncated AbnA (domains 1-3), a GH43 arabinanase from
RT Geobacilllus stearothermophilus, in complex with arabinooctaose.";
RL Submitted (JAN-2016) to the PDB data bank.
RN [13] {ECO:0000313|EMBL:QOR82950.1, ECO:0000313|Proteomes:UP000593876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG-1 {ECO:0000313|EMBL:QOR82950.1,
RC ECO:0000313|Proteomes:UP000593876};
RA Ma T.;
RT "Genome of alkane degrading Geobacillus stearothermophilus SL-2 isolated
RT from a deep-subsurface oil reservoir.";
RL Submitted (OCT-2020) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ868502; ACE73680.1; -; Genomic_DNA.
DR EMBL; CP063162; QOR82950.1; -; Genomic_DNA.
DR PDB; 5HO0; X-ray; 2.35 A; A=1-848.
DR PDB; 5HO2; X-ray; 2.37 A; A=1-848.
DR PDB; 5HO9; X-ray; 2.85 A; A/B=1-639.
DR PDB; 5HOF; X-ray; 2.96 A; A=1-848.
DR PDB; 5HON; X-ray; 2.00 A; A/B=640-848.
DR PDB; 5HP6; X-ray; 2.09 A; A=1-848.
DR PDBsum; 5HO0; -.
DR PDBsum; 5HO2; -.
DR PDBsum; 5HO9; -.
DR PDBsum; 5HOF; -.
DR PDBsum; 5HON; -.
DR PDBsum; 5HP6; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR Proteomes; UP000593876; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; -; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5HO0, ECO:0007829|PDB:5HO2};
KW Calcium {ECO:0007829|PDB:5HO0, ECO:0007829|PDB:5HO2};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:QOR82950.1};
KW Metal-binding {ECO:0007829|PDB:5HO0, ECO:0007829|PDB:5HO2};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..848
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041156517"
FT DOMAIN 708..838
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT ACT_SITE 55
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 304
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:5HO0, ECO:0007829|PDB:5HO2"
FT BINDING 649
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5HO0, ECO:0007829|PDB:5HO2"
FT BINDING 651
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5HO0, ECO:0007829|PDB:5HO2"
FT BINDING 686
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5HO0, ECO:0007829|PDB:5HO2"
FT BINDING 688
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5HO0, ECO:0007829|PDB:5HO2"
FT BINDING 826
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5HO0, ECO:0007829|PDB:5HO2"
FT BINDING 827
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5HO0, ECO:0007829|PDB:5HO2"
FT SITE 238
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 848 AA; 94027 MW; 22E29EEC4254F61F CRC64;
MKRRSLKGIA LFLLIVAVCL SSATLGRGEE KHTGENVRQN QKVKDPQFTN VSVHDPSIVK
DGDTYYIFGS HIEAAKSKDL MNWEKFTNGY TTPNNKLYGD LSKNLAGSFK WAGENDADSK
GGFAVWAPDV FWNKDYVNED GTKGAYMIYY SVSSTYIRSA IGYAVSKHIE GPYKYVDTIV
YSGFTKEEAY DANSKINKKW TNTNIPKLIE QGKLKGVRAD WFHNDGSYNN RDFPNAIDPN
LFYDEKGNLW MAYGSWSGGI FVLPMDKTTG KPIYPGKDGK TPDGRLVDRY FGIKIAGGYY
QSGEGTYIVY DKNTDYYYLY VTYGWLGADG GYNMRQFRST SPTGPYVDAK GQSAVLPGEV
DNSPYGNKIM GNFLFERKVG DPGTGIGVGY VSPGHNSVYL DRKTGQQFLV FHTRFPQSGE
YHEVRVHQMF MNKNGWPVVA PYRYAGEKLE KVNKQDVVGE YQLINHGKDY SADIKKQIFV
RLNRNNTISG DATGTWRKIG HNQAEITIDG ETYDGVFVRQ WDPTSKRYVM AFTALSNEGV
SIWGSKLADK TDEEIVEDVA SDLDLGDTDH VVSNLHLPTE GTRHTVISWT TSDAKVVSET
GVVHRPEVGS APVTATLTAT ITKGDATATK VFHITVLPYE EAKLTAHYSF DNNDLSDSTG
NFGPGTITGN RIDNEGGTIA YADGKIGKAA VLNGQSGIRL PDGLVSSNQY SVSLWVKPEQ
LTTHTTTFFG AKDPNHWISL VPQGWDGNTM LWSGSSPWYD GRTFWKIPTG QWTHLAFSVD
NGAVKVYING VEKFSGTNFP DVFTGANASF ALGVNWWDPP FKGLIDELRI YEGALTPSQV
TDLAQTSE
//
