ID   MANA_RHOM4              Reviewed;         558 AA.
AC   P49425; D0MK12;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 3.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase;
DE            EC=3.2.1.78;
DE   AltName: Full=Endo-(1,4)-beta-mannanase;
GN   Name=manA; OrderedLocusNames=Rmar_0016;
OS   Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS   obamensis).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Rhodothermus.
OX   NCBI_TaxID=518766;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=10919332; DOI=10.1007/s002530000351;
RA   Politz O., Krah M., Thomsen K.K., Borriss R.;
RT   "A highly thermostable endo-(1,4)-beta-mannanase from the marine bacterium
RT   Rhodothermus marinus.";
RL   Appl. Microbiol. Biotechnol. 53:715-721(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43812 / DSM 4252 / R-10;
RX   PubMed=21304669; DOI=10.4056/sigs.46736;
RA   Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA   Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Detter J.C.;
RT   "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL   Stand. Genomic Sci. 1:283-291(2009).
CC   -!- FUNCTION: Acts as endo-acting enzyme with a requirement for at least
CC       five sugar moieties for effective catalytic activity. Hydrolyzes carob-
CC       galactomannan (locust bean gum) effectively and to a smaller extent
CC       guar gum, but not yeast mannan. {ECO:0000269|PubMed:10919332}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC         mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.4. {ECO:0000269|PubMed:10919332};
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius.
CC         {ECO:0000269|PubMed:10919332};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01100, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA62442.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X90947; CAA62442.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001807; ACY46925.1; -; Genomic_DNA.
DR   PIR; T10748; T10748.
DR   RefSeq; WP_012842537.1; NC_013501.1.
DR   AlphaFoldDB; P49425; -.
DR   SMR; P49425; -.
DR   STRING; 518766.Rmar_0016; -.
DR   CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR   CAZy; GH26; Glycoside Hydrolase Family 26.
DR   EnsemblBacteria; ACY46925; ACY46925; Rmar_0016.
DR   KEGG; rmr:Rmar_0016; -.
DR   eggNOG; COG4124; Bacteria.
DR   HOGENOM; CLU_016930_1_1_10; -.
DR   OMA; WGWYLID; -.
DR   OrthoDB; 669354at2; -.
DR   BRENDA; 3.2.1.78; 5425.
DR   Proteomes; UP000002221; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR022790; GH26_dom.
DR   InterPro; IPR000805; Glyco_hydro_26.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR026444; Secre_tail.
DR   PANTHER; PTHR40079; PTHR40079; 1.
DR   Pfam; PF02156; Glyco_hydro_26; 1.
DR   PRINTS; PR00739; GLHYDRLASE26.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR04183; Por_Secre_tail; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS51764; GH26; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..558
FT                   /note="Mannan endo-1,4-beta-mannosidase"
FT                   /id="PRO_0000057685"
FT   DOMAIN          17..137
FT                   /note="CBM6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   DOMAIN          153..455
FT                   /note="GH26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        313
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        406
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
SQ   SEQUENCE   558 AA;  63120 MW;  E977F92CEE320807 CRC64;
     MTLLLVWLIF TGVAGEIRLE AEDGELLGVA VDSTLTGYSG RGYVTGFDAP EDSVRFSFEA
     PRGVYRVVFG VSFSSRFASY ALRVDDWHQT GSLIKRGGGF FEASIGEIWL DEGAHTMAFQ
     LMNGALDYVR LEPVSYGPPA RPPAQLSDSQ ATASAQALFA FLLSEYGRHI LAGQQQNPYR
     RDFDAINYVR NVTGKEPALV SFDLIDYSPT REAHGVVHYQ TPEDWIAWAG RDGIVSLMWH
     WNAPTDLIED PSQDCYWWYG FYTRCTTFDV AAALADTSSE RYRLLLRDID VIAAQLQKFQ
     QADIPVLWRP LHEAAGGWFW WGAKGPEPFK QLWRLLYERL VHHHGLHNLI WVYTHEPGAA
     EWYPGDAYVD IVGRDVYADD PDALMRSDWN ELQTLFGGRK LVALTETGTL PDVEVITDYG
     IWWSWFSIWT DPFLRDVDPD RLTRVYHSER VLTRDELPDW RSYVLHATTV QPAGDLALAV
     YPNPGAGRLH VEVGLPVAAP VVVEVFNLLG QRVFQYQAGM QPAGLWRRAF ELALAPGVYL
     VQVRAGNLVA RRRWVSVR