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O05511 (MANA2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable mannose-6-phosphate isomerase GmuF

EC=5.3.1.8
Alternative name(s):
Glucomannan utilization protein F
Phosphohexomutase
Phosphomannose isomerase
Short name=PMI
Gene names
Name:gmuF
Synonyms:ydhS
Ordered Locus Names:BSU05870
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to be involved in the degradation of glucomannan. Ref.3

Catalytic activity

D-mannose 6-phosphate = D-fructose 6-phosphate.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Induction

Up-regulated by konjac glucomannan and by cellobiose and mannobiose, the possible degradation products of glucomannan. Repressed by glucose via the carbon catabolite repression system. Also repressed by GmuR. Ref.3

Sequence similarities

Belongs to the mannose-6-phosphate isomerase type 1 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmannose-6-phosphate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 315315Probable mannose-6-phosphate isomerase GmuF
PRO_0000372435

Sites

Active site1921 By similarity
Metal binding951Zinc By similarity
Metal binding971Zinc By similarity
Metal binding1151Zinc By similarity
Metal binding1721Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
O05511 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: ED6F1855D41B4DDF

FASTA31535,492
        10         20         30         40         50         60 
MTHPLFLEPV FKERLWGGTK LRDAFGYAIP SQKTGECWAV SAHAHGSSSV KNGPLAGKTL 

        70         80         90        100        110        120 
DQVWKDHPEI FGFPDGKVFP LLVKLLDANM DLSVQVHPDD DYAKLHENGD LGKTECWYII 

       130        140        150        160        170        180 
DCKDDAELIL GHHASTKEEF KQRIESGDWN GLLRRIKIKP GDFFYVPSGT LHALCKGTLV 

       190        200        210        220        230        240 
LEIQQNSDTT YRVYDYDRCN DQGQKRTLHI EKAMEVITIP HIDKVHTPEV KEVGNAEIIV 

       250        260        270        280        290        300 
YVQSDYFSVY KWKISGRAAF PSYQTYLLGS VLSGSGRIIN NGIQYECNAG SHFILPAHFG 

       310 
EFTIEGTCEF MISHP 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the Bacillus subtilis chromosome."
Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y., Ogasawara N.
Microbiology 143:1861-1866(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Glucomannan utilization operon of Bacillus subtilis."
Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K.
FEMS Microbiol. Lett. 279:103-109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, FUNCTION IN GLUCOMANNAN UTILIZATION.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88802 Genomic DNA. Translation: BAA19711.1.
AL009126 Genomic DNA. Translation: CAB12406.1.
PIRG69785.
RefSeqNP_388468.1. NC_000964.3.

3D structure databases

ProteinModelPortalO05511.
SMRO05511. Positions 2-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU05870.

Proteomic databases

PaxDbO05511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12406; CAB12406; BSU05870.
GeneID938028.
KEGGbsu:BSU05870.
PATRIC18972790. VBIBacSub10457_0616.

Organism-specific databases

GenoListBSU05870. [Micado]

Phylogenomic databases

eggNOGCOG1482.
HOGENOMHOG000054245.
KOK01809.
OMADFFTMVK.
OrthoDBEOG66MQQS.
ProtClustDBCLSK2752329.

Enzyme and pathway databases

BioCycBSUB:BSU05870-MONOMER.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
InterProIPR001250. Man6P_Isoase-1.
IPR014628. Man6P_isomerase_Firm_short.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERPTHR18964:SF1. PTHR18964:SF1. 1 hit.
PfamPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFPIRSF036894. PMI_Firm_short. 1 hit.
SUPFAMSSF51182. SSF51182. 1 hit.
TIGRFAMsTIGR00218. manA. 2 hits.
ProtoNetSearch...

Entry information

Entry nameMANA2_BACSU
AccessionPrimary (citable) accession number: O05511
Secondary accession number(s): Q797D7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: July 1, 1997
Last modified: February 19, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList