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O05511

- MANA2_BACSU

UniProt

O05511 - MANA2_BACSU

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Protein

Probable mannose-6-phosphate isomerase GmuF

Gene

gmuF

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Seems to be involved in the degradation of glucomannan.1 Publication

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi95 – 951ZincBy similarity
Metal bindingi97 – 971ZincBy similarity
Metal bindingi115 – 1151ZincBy similarity
Metal bindingi172 – 1721ZincBy similarity
Active sitei192 – 1921By similarity

GO - Molecular functioni

  1. mannose-6-phosphate isomerase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU05870-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:gmuF
Synonyms:ydhS
Ordered Locus Names:BSU05870
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU05870. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Probable mannose-6-phosphate isomerase GmuFPRO_0000372435Add
BLAST

Proteomic databases

PaxDbiO05511.

Expressioni

Inductioni

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.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU05870.

Structurei

3D structure databases

ProteinModelPortaliO05511.
SMRiO05511. Positions 2-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1482.
HOGENOMiHOG000054245.
InParanoidiO05511.
KOiK01809.
OMAiPLATHIF.
OrthoDBiEOG66MQQS.
PhylomeDBiO05511.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR001250. Man6P_Isoase-1.
IPR014628. Man6P_isomerase_Firm_short.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFiPIRSF036894. PMI_Firm_short. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR00218. manA. 2 hits.

Sequencei

Sequence statusi: Complete.

O05511-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTHPLFLEPV FKERLWGGTK LRDAFGYAIP SQKTGECWAV SAHAHGSSSV
60 70 80 90 100
KNGPLAGKTL DQVWKDHPEI FGFPDGKVFP LLVKLLDANM DLSVQVHPDD
110 120 130 140 150
DYAKLHENGD LGKTECWYII DCKDDAELIL GHHASTKEEF KQRIESGDWN
160 170 180 190 200
GLLRRIKIKP GDFFYVPSGT LHALCKGTLV LEIQQNSDTT YRVYDYDRCN
210 220 230 240 250
DQGQKRTLHI EKAMEVITIP HIDKVHTPEV KEVGNAEIIV YVQSDYFSVY
260 270 280 290 300
KWKISGRAAF PSYQTYLLGS VLSGSGRIIN NGIQYECNAG SHFILPAHFG
310
EFTIEGTCEF MISHP
Length:315
Mass (Da):35,492
Last modified:July 1, 1997 - v1
Checksum:iED6F1855D41B4DDF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D88802 Genomic DNA. Translation: BAA19711.1.
AL009126 Genomic DNA. Translation: CAB12406.1.
PIRiG69785.
RefSeqiNP_388468.1. NC_000964.3.
WP_003242491.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB12406; CAB12406; BSU05870.
GeneIDi938028.
KEGGibsu:BSU05870.
PATRICi18972790. VBIBacSub10457_0616.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D88802 Genomic DNA. Translation: BAA19711.1 .
AL009126 Genomic DNA. Translation: CAB12406.1 .
PIRi G69785.
RefSeqi NP_388468.1. NC_000964.3.
WP_003242491.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali O05511.
SMRi O05511. Positions 2-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU05870.

Proteomic databases

PaxDbi O05511.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12406 ; CAB12406 ; BSU05870 .
GeneIDi 938028.
KEGGi bsu:BSU05870.
PATRICi 18972790. VBIBacSub10457_0616.

Organism-specific databases

GenoListi BSU05870. [Micado ]

Phylogenomic databases

eggNOGi COG1482.
HOGENOMi HOG000054245.
InParanoidi O05511.
KOi K01809.
OMAi PLATHIF.
OrthoDBi EOG66MQQS.
PhylomeDBi O05511.

Enzyme and pathway databases

BioCyci BSUB:BSU05870-MONOMER.

Family and domain databases

Gene3Di 2.60.120.10. 2 hits.
InterProi IPR001250. Man6P_Isoase-1.
IPR014628. Man6P_isomerase_Firm_short.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view ]
Pfami PF01238. PMI_typeI. 1 hit.
[Graphical view ]
PIRSFi PIRSF036894. PMI_Firm_short. 1 hit.
SUPFAMi SSF51182. SSF51182. 1 hit.
TIGRFAMsi TIGR00218. manA. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiMANA2_BACSU
AccessioniPrimary (citable) accession number: O05511
Secondary accession number(s): Q797D7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 92 of the entry and version 1 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3