ID B8CZV1_HALOH Unreviewed; 315 AA.
AC B8CZV1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Glycoside hydrolase family 43 {ECO:0000313|EMBL:ACL70803.1};
GN OrderedLocusNames=Hore_20580 {ECO:0000313|EMBL:ACL70803.1};
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL70803.1, ECO:0000313|Proteomes:UP000000719};
RN [1] {ECO:0000313|EMBL:ACL70803.1, ECO:0000313|Proteomes:UP000000719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
RN [2] {ECO:0007829|PDB:4QQS}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS).
RX PubMed=25760712; DOI=10.1107/S2053230X15003337;
RA Hassan N., Kori L.D., Gandini R., Patel B.K., Divne C., Tan T.C.;
RT "High-resolution crystal structure of a polyextreme GH43 glycosidase from
RT Halothermothrix orenii with alpha-L-arabinofuranosidase activity.";
RL Acta Crystallogr. F Struct. Biol. Commun. 71:338-345(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP001098; ACL70803.1; -; Genomic_DNA.
DR RefSeq; WP_015923772.1; NC_011899.1.
DR PDB; 4QQS; X-ray; 1.10 A; A/B=1-315.
DR PDBsum; 4QQS; -.
DR AlphaFoldDB; B8CZV1; -.
DR SMR; B8CZV1; -.
DR STRING; 373903.Hore_20580; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR KEGG; hor:Hore_20580; -.
DR eggNOG; COG3940; Bacteria.
DR HOGENOM; CLU_009397_4_0_9; -.
DR OrthoDB; 273314at2; -.
DR BRENDA; 3.2.1.55; 7869.
DR Proteomes; UP000000719; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08991; GH43_HoAraf43-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4QQS};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000000719};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT ACT_SITE 17
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 195
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 126
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 315 AA; 35534 MW; B3B956A3239FFD59 CRC64;
MKDTYTNPVG GITGIGDPYV LKHESRYYLY ATSAINRGFK VWESPNLVDW ELKGLALDSY
YEKNGWGTED FWAPEVIFYN NKFYMTYSAR DNDGHLKIAL ASSKSPLGPF KNIKAPLFDR
GLSFIDAHIF IDQDGTPYIY YVKDCSENII NGIHISQIYV QEMSQDLLEL KGDPVLAIQP
SQDWEGINDA WQWNEGPFVI KHEGKYYMMY SANCYASPDY SIGYAVAETP LGPWIKYSGN
PILSKRMDKG ISGPGHNSVT VSPDGSELFV VYHTHTYPDS PGGDRTVNID RLYFEDGILK
VKGPTRSPQP GPRSN
//
