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P49425

- MANA_RHOM4

UniProt

P49425 - MANA_RHOM4

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Protein

Mannan endo-1,4-beta-mannosidase

Gene

manA

Organism
Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus obamensis)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

pH dependencei

Optimum pH is 5.4.1 Publication

Temperature dependencei

Optimum temperature is 85 degrees Celsius.1 Publication

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. cellulase activity Source: InterPro
  3. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. substituted mannan metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciRMAR518766:GJJ8-18-MONOMER.
BRENDAi3.2.1.78. 5425.

Protein family/group databases

CAZyiCBM35. Carbohydrate-Binding Module Family 35.
GH26. Glycoside Hydrolase Family 26.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannan endo-1,4-beta-mannosidase (EC:3.2.1.78)
Alternative name(s):
Endo-(1,4)-beta-mannanase
Gene namesi
Name:manA
Ordered Locus Names:Rmar_0016
OrganismiRhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus obamensis)
Taxonomic identifieri518766 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeRhodothermus
ProteomesiUP000002221: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Mannan endo-1,4-beta-mannosidasePRO_0000057685Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi518766.Rmar_0016.

Structurei

3D structure databases

ProteinModelPortaliP49425.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 137121CBM6PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 26 family.Curated
Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG4124.
HOGENOMiHOG000235025.
OrthoDBiEOG66HVDV.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR005084. 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]
PfamiPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSiPR00739. GLHYDRLASE26.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR04183. Por_Secre_tail. 1 hit.
PROSITEiPS51175. CBM6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49425-1 [UniParc]FASTAAdd to Basket

« Hide

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

RRRWVSVR
Length:558
Mass (Da):63,120
Last modified:January 19, 2010 - v3
Checksum:iE977F92CEE320807
GO

Sequence cautioni

The sequence CAA62442.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90947 Genomic DNA. Translation: CAA62442.1. Different initiation.
CP001807 Genomic DNA. Translation: ACY46925.1.
PIRiT10748.
RefSeqiYP_003289313.1. NC_013501.1.

Genome annotation databases

EnsemblBacteriaiACY46925; ACY46925; Rmar_0016.
GeneIDi8566638.
KEGGirmr:Rmar_0016.
PATRICi32314039. VBIRhoMar93821_0016.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90947 Genomic DNA. Translation: CAA62442.1 . Different initiation.
CP001807 Genomic DNA. Translation: ACY46925.1 .
PIRi T10748.
RefSeqi YP_003289313.1. NC_013501.1.

3D structure databases

ProteinModelPortali P49425.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 518766.Rmar_0016.

Protein family/group databases

CAZyi CBM35. Carbohydrate-Binding Module Family 35.
GH26. Glycoside Hydrolase Family 26.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACY46925 ; ACY46925 ; Rmar_0016 .
GeneIDi 8566638.
KEGGi rmr:Rmar_0016.
PATRICi 32314039. VBIRhoMar93821_0016.

Phylogenomic databases

eggNOGi COG4124.
HOGENOMi HOG000235025.
OrthoDBi EOG66HVDV.

Enzyme and pathway databases

BioCyci RMAR518766:GJJ8-18-MONOMER.
BRENDAi 3.2.1.78. 5425.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProi 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 ]
Pfami PF02156. Glyco_hydro_26. 1 hit.
[Graphical view ]
PRINTSi PR00739. GLHYDRLASE26.
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
TIGRFAMsi TIGR04183. Por_Secre_tail. 1 hit.
PROSITEi PS51175. CBM6. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43812 / DSM 4252 / R-10.

Entry informationi

Entry nameiMANA_RHOM4
AccessioniPrimary (citable) accession number: P49425
Secondary accession number(s): D0MK12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 19, 2010
Last modified: November 26, 2014
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3