EABN_THEP1
ID EABN_THEP1 Reviewed; 471 AA.
AC A5IKD4;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Extracellular endo-alpha-(1->5)-L-arabinanase;
DE Short=ABN;
DE EC=3.2.1.99;
DE AltName: Full=Endo-1,5-alpha-L-arabinanase;
DE Flags: Precursor;
GN OrderedLocusNames=Tpet_0637;
OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS RKU-1).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=390874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermotoga petrophila RKU-1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=20678476; DOI=10.1016/j.bbrc.2010.07.097;
RA Squina F.M., Santos C.R., Ribeiro D.A., Cota J., de Oliveira R.R.,
RA Ruller R., Mort A., Murakami M.T., Prade R.A.;
RT "Substrate cleavage pattern, biophysical characterization and low-
RT resolution structure of a novel hyperthermostable arabinanase from
RT Thermotoga petrophila.";
RL Biochem. Biophys. Res. Commun. 399:505-511(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 21-471, AND ACTIVE SITE.
RX PubMed=24469445; DOI=10.1074/jbc.m113.537167;
RA Santos C.R., Polo C.C., Costa M.C., Nascimento A.F., Meza A.N., Cota J.,
RA Hoffmam Z.B., Honorato R.V., Oliveira P.S., Goldman G.H., Gilbert H.J.,
RA Prade R.A., Ruller R., Squina F.M., Wong D.W., Murakami M.T.;
RT "Mechanistic strategies for catalysis adopted by evolutionary distinct
RT family 43 arabinanases.";
RL J. Biol. Chem. 289:7362-7373(2014).
CC -!- FUNCTION: Involved in the degradation of arabinan and is a key enzyme
CC in the complete degradation of the plant cell wall. Catalyzes the
CC internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues in
CC different arabinan-containing polysaccharides, and releases
CC arabinotriose and arabinobiose as end products. It acts on branched
CC arabinan (from sugar beet), but more slowly when compared to linear or
CC debranched arabinan. {ECO:0000269|PubMed:20678476}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC (1->5)-arabinans.; EC=3.2.1.99;
CC Evidence={ECO:0000269|PubMed:20678476};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. It retains more than 75% activity over a pH range
CC from 4 to 7. {ECO:0000269|PubMed:20678476};
CC Temperature dependence:
CC Optimum temperature is 73 degrees Celsius. It is fully heat-stable
CC (up to 10 hours) and retains activity at temperatures up to 90
CC degrees Celsius. The enzyme loses its activity only after 90 minutes
CC when incubated at 95 degrees Celsius. {ECO:0000269|PubMed:20678476};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20678476}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- MISCELLANEOUS: Although it functions as an extracellular endo-alpha-
CC (1->5)-L-arabinanase, its sequence is quite divergent from the
CC B.subtilis enzyme.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR EMBL; CP000702; ABQ46657.1; -; Genomic_DNA.
DR PDB; 4KC7; X-ray; 1.75 A; A/B/C=21-471.
DR PDB; 4KC8; X-ray; 1.76 A; A/B/C=21-471.
DR PDBsum; 4KC7; -.
DR PDBsum; 4KC8; -.
DR AlphaFoldDB; A5IKD4; -.
DR SMR; A5IKD4; -.
DR STRING; 390874.Tpet_0637; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR EnsemblBacteria; ABQ46657; ABQ46657; Tpet_0637.
DR KEGG; tpt:Tpet_0637; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_1_2_0; -.
DR OMA; MNPKTGF; -.
DR BRENDA; 3.2.1.99; 11620.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000006558; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR032291; Abn2_C.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF16369; GH43_C; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Metal-binding; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..471
FT /note="Extracellular endo-alpha-(1->5)-L-arabinanase"
FT /id="PRO_5000246952"
FT ACT_SITE 32
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:24469445"
FT ACT_SITE 223
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:24469445"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:24469445"
FT BINDING 167..170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187..189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219..223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 170
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 314
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000250"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:4KC7"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4KC7"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:4KC7"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:4KC7"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:4KC7"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4KC7"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 221..229
FT /evidence="ECO:0007829|PDB:4KC7"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 236..246
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:4KC7"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:4KC7"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 308..319
FT /evidence="ECO:0007829|PDB:4KC7"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:4KC7"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 397..401
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 421..428
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 431..443
FT /evidence="ECO:0007829|PDB:4KC7"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 449..458
FT /evidence="ECO:0007829|PDB:4KC7"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:4KC7"
SQ SEQUENCE 471 AA; 53463 MW; 64DE1C376E9CE417 CRC64;
MRFLFLMITL TALTGYILAD EQPTFRWAVV HDPSIIKVGN MYYVFGTHLQ VAKSKDLMHW
EQINTSAHDK NPIIPNINEE LKETLSWART RNDIWAPQVI QLSDGRYYMY YCASTFGSPR
SAIGIAVSDD IEGPYKHYAV IVKSGQVYSV DGPSEDGTPY DSRKHPNALD PGVFYDKEGN
LWMVYGSWFG GIYILKLDPN TGLPLPGQGY GKRLVGGNHS SMEGPYILYS PDTDYYYLFL
SFGGLDYRGG YNIRVARSKN PNGPYYDPEG KSMENCMGSK TVISNYGAKL VGNFILSESN
TIDFKAFGYV SPGHNSAYYD PETGKYFIFF HTRFPGRGET YQLRVHQLFL NEDGWFVMAP
FPYGGETVSK LPNEEIVGEY QFINHGKEIT DKIKQPVRIK LNSDGSITGA VEGRWERKEH
YITLKIIEGN TTVIYKGVLL KQWHYSEKKW VTVFTALSNQ GVSVWGIRVE E
