Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mannose-6-phosphate isomerase ManA

Gene

manA

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

Functioni

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi97 – 971ZincBy similarity
Metal bindingi110 – 1101ZincBy similarity
Metal bindingi172 – 1721ZincBy similarity
Active sitei192 – 1921By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU12020-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannose-6-phosphate isomerase ManA (EC:5.3.1.8)
Alternative name(s):
Phosphohexomutase
Phosphomannose isomerase
Short name:
PMI
Gene namesi
Name:manA
Synonyms:pmi, yjdE
Ordered Locus Names:BSU12020
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU12020. [Micado]

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are unable to grow in minimal medium with mannose as the sole carbon source. They show impaired growth in rich medium, and impairment increases in the presence of greater than 1.4 mM mannose.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Mannose-6-phosphate isomerase ManAPRO_0000371314Add
BLAST

Proteomic databases

PaxDbiO31646.

Expressioni

Inductioni

Up-regulated by mannose. Is under the control of ManR. Is subject to carbon catabolite repression (CCR) by glucose. Forms part of an operon with manP and yjdF.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100006646.

Structurei

3D structure databases

ProteinModelPortaliO31646.
SMRiO31646. Positions 2-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1482.
HOGENOMiHOG000054245.
InParanoidiO31646.
KOiK01809.
OMAiAFIISGH.
OrthoDBiEOG66MQQS.
PhylomeDBiO31646.

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.

O31646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTEPLFFKP VFKERIWGGT ALADFGYTIP SQRTGECWAF AAHQNGQSVV
60 70 80 90 100
QNGMYKGFTL SELWEHHRHL FGQLEGDRFP LLTKILDADQ DLSVQVHPND
110 120 130 140 150
EYANIHENGE LGKTECWYII DCQKDAEIIY GHNATTKEEL TTMIERGEWD
160 170 180 190 200
ELLRRVKVKP GDFFYVPSGT VHAIGKGILA LETQQNSDTT YRLYDYDRKD
210 220 230 240 250
AEGKLRELHL KKSIEVIEVP SIPERHTVHH EQIEDLLTTT LIECAYFSVG
260 270 280 290 300
KWNLSGSASL KQQKPFLLIS VIEGEGRMIS GEYVYPFKKG DHMLLPYGLG
310
EFKLEGYAEC IVSHL
Length:315
Mass (Da):36,003
Last modified:January 1, 1998 - v1
Checksum:i6848958CF5545064
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13059.1.
PIRiH69848.
RefSeqiNP_389084.1. NC_000964.3.
WP_003232833.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13059; CAB13059; BSU12020.
GeneIDi939393.
KEGGibsu:BSU12020.
PATRICi18974133. VBIBacSub10457_1259.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13059.1.
PIRiH69848.
RefSeqiNP_389084.1. NC_000964.3.
WP_003232833.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliO31646.
SMRiO31646. Positions 2-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100006646.

Proteomic databases

PaxDbiO31646.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13059; CAB13059; BSU12020.
GeneIDi939393.
KEGGibsu:BSU12020.
PATRICi18974133. VBIBacSub10457_1259.

Organism-specific databases

GenoListiBSU12020. [Micado]

Phylogenomic databases

eggNOGiCOG1482.
HOGENOMiHOG000054245.
InParanoidiO31646.
KOiK01809.
OMAiAFIISGH.
OrthoDBiEOG66MQQS.
PhylomeDBiO31646.

Enzyme and pathway databases

BioCyciBSUB:BSU12020-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis."
    Reizer J., Bachem S., Reizer A., Arnaud M., Saier M.H. Jr., Stuelke J.
    Microbiology 145:3419-3429(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME.
    Strain: 168.
  3. "Mutations in multidrug efflux homologs, sugar isomerases, and antimicrobial biosynthesis genes differentially elevate activity of the sigma(X) and sigma(W) factors in Bacillus subtilis."
    Turner M.S., Helmann J.D.
    J. Bacteriol. 182:5202-5210(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: 168.
  4. "Characterization of a mannose utilization system in Bacillus subtilis."
    Sun T., Altenbuchner J.
    J. Bacteriol. 192:2128-2139(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiMANA1_BACSU
AccessioniPrimary (citable) accession number: O31646
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: January 1, 1998
Last modified: July 22, 2015
This is version 96 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.