ID   Q97LI4_CLOAB            Unreviewed;       676 AA.
AC   Q97LI4;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   02-SEP-2026, entry version 122.
DE   SubName: Full=Endo-arabinase related enzyme (Family 43 glycosyl hydrolase domain and ricin B-like domain) {ECO:0000313|EMBL:AAK78555.1};
GN   OrderedLocusNames=CA_C0577 {ECO:0000313|EMBL:AAK78555.1};
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM
OS   19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK78555.1, ECO:0000313|Proteomes:UP000000814};
RN   [1] {ECO:0000313|EMBL:AAK78555.1, ECO:0000313|Proteomes:UP000000814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC   {ECO:0000313|Proteomes:UP000000814};
RX   PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00174}.
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DR   EMBL; AE001437; AAK78555.1; -; Genomic_DNA.
DR   PIR; H96970; H96970.
DR   RefSeq; WP_010963897.1; NC_003030.1.
DR   AlphaFoldDB; Q97LI4; -.
DR   STRING; 272562.CA_C0577; -.
DR   GeneID; 44997088; -.
DR   KEGG; cac:CA_C0577; -.
DR   PATRIC; fig|272562.8.peg.780; -.
DR   eggNOG; COG3507; Bacteria.
DR   HOGENOM; CLU_009397_1_2_9; -.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000000814; 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; cd00161; beta-trefoil_Ricin-like; 1.
DR   CDD; cd18832; GH43_GsAbnA-like; 1.
DR   Gene3D; 2.40.128.10; -; 1.
DR   Gene3D; 2.80.10.50; -; 3.
DR   Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 1.
DR   InterPro; IPR032291; Abn2_C.
DR   InterPro; IPR050727; GH43_arabinanases.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF3; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE A-RELATED; 1.
DR   Pfam; PF16369; GH43_C; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   Pfam; PF14200; RicinB_lectin_2; 2.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAK78555.1};
KW   Lectin {ECO:0000256|PROSITE-ProRule:PRU00174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000814}.
FT   DOMAIN          534..674
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   ACT_SITE        48
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        267
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            203
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   676 AA;  74509 MW;  E28AB456D8D309F3 CRC64;
     MKNKFKKIIS ITLGLSLTFV TQLNLIPFGN EVTAFAAALN TSRVSVHDPS IAQAGGKYYL
     FGSHRADAVS SDLASWNYFQ TNINNDYANI FSVGGKWAAH GSNSYDITGN LWAPDVIYNP
     QMKKWCIYMS VNGDKFYSSI ALATSNNITG PYKYAGTIVY SGFTNSSLAS QTDYSKVTGT
     NNVASRYLSK GAWNSSYGPN AIDPCVKYDK SGNLWLSYGS WFGGIFMLKL DKSTGLRDYS
     YTYSTKTNAS DQYLGIKISG GYGTCGEGSY IVYDKATDYY YLYESYCGLD ATDNFSGYHI
     RLFRSKNITG PYTDAKGNPA ICTSANDNKS NKGIKLFGNY YFSSLSSVNG SELSSKGYMS
     GGHNSAIIDT SGQRYLIYHT RFNNGTEAHQ IRVHQQFLNE DGWPVTAVYE YLGSQISKSG
     YSSNDIIGTY EFINHGLNAT TAKTGMLKTS KVSLNANGSI SGDYTGTWVE KSGSYYCNMV
     IGGITYKGIF FKQYDESASH KNTMTFSLIG SNNESIWGSK ISGSTINPSP KLDGTYYIKS
     SLSGMYLDVA NGQNTDGTNI RQWTPLNNNA QKFKIVSDSD GCYHILTGAS NYKSCIDVTN
     NSSSNGSNIE EWSYWNGDMQ KFKIQKVSEN KYAILTKSSN FKSCLDVYNM SKDSGANVCQ
     WNYWGGNGQL WELIPN
//