ID   A5TYD3_MYCTA            Unreviewed;       380 AA.
AC   A5TYD3;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   02-SEP-2026, entry version 82.
DE   RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN   Name=celA1 {ECO:0000313|EMBL:ABQ71783.1};
GN   OrderedLocusNames=MRA_0064 {ECO:0000313|EMBL:ABQ71783.1};
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947 {ECO:0000313|EMBL:ABQ71783.1, ECO:0000313|Proteomes:UP000001988};
RN   [1] {ECO:0000313|EMBL:ABQ71783.1, ECO:0000313|Proteomes:UP000001988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra {ECO:0000313|Proteomes:UP000001988};
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC       {ECO:0000256|RuleBase:RU361186}.
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DR   EMBL; CP000611; ABQ71783.1; -; Genomic_DNA.
DR   RefSeq; WP_003400562.1; NC_009525.1.
DR   AlphaFoldDB; A5TYD3; -.
DR   SMR; A5TYD3; -.
DR   KEGG; mra:MRA_0064; -.
DR   eggNOG; COG5297; Bacteria.
DR   HOGENOM; CLU_015488_2_2_11; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR   FunFam; 3.20.20.40:FF:000004; Glucanase; 1.
DR   Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1.
DR   InterPro; IPR016288; Beta_cellobiohydrolase.
DR   InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR   PANTHER; PTHR34876; -; 1.
DR   PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1.
DR   Pfam; PF01341; Glyco_hydro_6; 1.
DR   PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR   PRINTS; PR00733; GLHYDRLASE6.
DR   SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361186};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361186};
KW   Glycosidase {ECO:0000256|RuleBase:RU361186};
KW   Hydrolase {ECO:0000256|RuleBase:RU361186};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361186};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001988};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        206
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT   ACT_SITE        353
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-1"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
FT   BINDING         351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001100-2"
SQ   SEQUENCE   380 AA;  39974 MW;  AAA8F1BD10C4CB68 CRC64;
     MTRRTGQRWR GTLPGRRPWT RPAPATCRRH LAFVELRHYF ARVMSSAIGS VARWIVPLLG
     VAAVASIGVI ADPVRVVRAP ALILVDAANP LAGKPFYVDP ASAAMVAARN ANPPNAELTS
     VANTPQSYWL DQAFPPATVG GTVARYTGAA QAAGAMPVLT LYGIPHRDCG SYASGGFATG
     TDYRGWIDAV ASGLGSSPAT IIVEPDALAM ADCLSPDQRQ ERFDLVRYAV DTLTRDPAAA
     VYVDAGHSRW LSAEAMAARL NDVGVGRARG FSLNVSNFYT TDEEIGYGEA ISGLTNGSHY
     VIDTSRNGAG PAPDAPLNWC NPSGRALGAP PTTATAGAHA DAYLWIKRPG ESDGTCGRGE
     PQAGRFVSQY AIDLAHNAGQ
//