P49425 (MANA_RHOM4) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mannan endo-1,4-beta-mannosidase
EC=3.2.1.78

Alternative name(s):
Endo-(1,4)-beta-mannanase

Gene names

Name:	manA
Ordered Locus Names:	Rmar_0016

Organism

Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus obamensis) [Complete proteome] [HAMAP]

Taxonomic identifier

518766 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Bacteroidetes/Chlorobi group › Bacteroidetes › Bacteroidetes Order II. Incertae sedis › Rhodothermaceae › Rhodothermus › Rhodothermus marinus

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as endo-acting enzyme with a requirement for at least five sugar moieties for effective catalytic activity. Hydrolyzes carob-galactomannan (locust bean gum) effectively and to a smaller extent guar gum, but not yeast mannan. Ref.1
Catalytic activity	Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence similarities	Belongs to the glycosyl hydrolase 26 family. Contains 1 CBM6 (carbohydrate binding type-6) domain.
Biophysicochemical properties	pH dependence: Optimum pH is 5.4. Ref.1 Temperature dependence: Optimum temperature is 85 degrees Celsius.
Sequence caution	The sequence CAA62442.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	substituted mannan metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cellulase activity Inferred from electronic annotation. Source: InterPro mannan endo-1,4-beta-mannosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 558	558	Mannan endo-1,4-beta-mannosidase		PRO_0000057685
Regions
	Domain	17 – 137	121	CBM6

Sequences

	Sequence		Length	Mass (Da)
	P49425 [UniParc]. Last modified January 19, 2010. Version 3. Checksum: E977F92CEE320807	FASTA	558	63,120
	10 20 30 40 50 60 MTLLLVWLIF TGVAGEIRLE AEDGELLGVA VDSTLTGYSG RGYVTGFDAP EDSVRFSFEA 70 80 90 100 110 120 PRGVYRVVFG VSFSSRFASY ALRVDDWHQT GSLIKRGGGF FEASIGEIWL DEGAHTMAFQ 130 140 150 160 170 180 LMNGALDYVR LEPVSYGPPA RPPAQLSDSQ ATASAQALFA FLLSEYGRHI LAGQQQNPYR 190 200 210 220 230 240 RDFDAINYVR NVTGKEPALV SFDLIDYSPT REAHGVVHYQ TPEDWIAWAG RDGIVSLMWH 250 260 270 280 290 300 WNAPTDLIED PSQDCYWWYG FYTRCTTFDV AAALADTSSE RYRLLLRDID VIAAQLQKFQ 310 320 330 340 350 360 QADIPVLWRP LHEAAGGWFW WGAKGPEPFK QLWRLLYERL VHHHGLHNLI WVYTHEPGAA 370 380 390 400 410 420 EWYPGDAYVD IVGRDVYADD PDALMRSDWN ELQTLFGGRK LVALTETGTL PDVEVITDYG 430 440 450 460 470 480 IWWSWFSIWT DPFLRDVDPD RLTRVYHSER VLTRDELPDW RSYVLHATTV QPAGDLALAV 490 500 510 520 530 540 YPNPGAGRLH VEVGLPVAAP VVVEVFNLLG QRVFQYQAGM QPAGLWRRAF ELALAPGVYL 550 VQVRAGNLVA RRRWVSVR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A highly thermostable endo-(1,4)-beta-mannanase from the marine bacterium Rhodothermus marinus." Politz O., Krah M., Thomsen K.K., Borriss R. Appl. Microbiol. Biotechnol. 53:715-721(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[2]	"Complete genome sequence of Rhodothermus marinus type strain (R-10)." Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A., Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G., Pati A. , Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C. Stand. Genomic Sci. 1:283-291(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43812 / DSM 4252 / R-10.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X90947 Genomic DNA. Translation: CAA62442.1. Different initiation. CP001807 Genomic DNA. Translation: ACY46925.1.
PIR	T10748.
RefSeq	YP_003289313.1. NC_013501.1.
3D structure databases
ProteinModelPortal	P49425.
ModBase	Search...
Protein-protein interaction databases
STRING	518766.Rmar_0016.
Protein family/group databases
CAZy	CBM35. Carbohydrate-Binding Module Family 35. GH26. Glycoside Hydrolase Family 26.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACY46925; ACY46925; Rmar_0016.
GeneID	8566638.
KEGG	rmr:Rmar_0016.
PATRIC	32314039. VBIRhoMar93821_0016.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4124.
HOGENOM	HOG000235025.
ProtClustDB	CLSK2823940.
Enzyme and pathway databases
BioCyc	RMAR518766:GJJ8-18-MONOMER.
BRENDA	3.2.1.78. 5425.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR005084. CMB_fam6. IPR022790. EndoGluc_H/Glyco_hydro_26. IPR008979. Galactose-bd-like. IPR000805. Glyco_hydro_26. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. IPR026444. Secre_tail. [Graphical view]
Pfam	PF02156. Glyco_hydro_26. 1 hit. [Graphical view]
PRINTS	PR00739. GLHYDRLASE26.
SUPFAM	SSF49785. Gal_bind_like. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
TIGRFAMs	TIGR04183. Por_Secre_tail. 1 hit.
PROSITE	PS51175. CBM6. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MANA_RHOM4

Accession

Primary (citable) accession number: P49425
Secondary accession number(s): D0MK12

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 19, 2010
Last modified:	May 1, 2013
This is version 68 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program