ID MANA1_BACSU Reviewed; 315 AA.
AC O31646;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 01-MAY-2013, entry version 81.
DE RecName: Full=Mannose-6-phosphate isomerase ManA;
DE EC=5.3.1.8;
DE AltName: Full=Phosphohexomutase;
DE AltName: Full=Phosphomannose isomerase;
DE Short=PMI;
GN Name=manA; Synonyms=pmi, yjdE; OrderedLocusNames=BSU12020;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP GENE NAME.
RC STRAIN=168;
RX PubMed=10627040;
RA Reizer J., Bachem S., Reizer A., Arnaud M., Saier M.H. Jr.,
RA Stuelke J.;
RT "Novel phosphotransferase system genes revealed by genome analysis -
RT the complete complement of PTS proteins encoded within the genome of
RT Bacillus subtilis.";
RL Microbiology 145:3419-3429(1999).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=10960106; DOI=10.1128/JB.182.18.5202-5210.2000;
RA Turner M.S., Helmann J.D.;
RT "Mutations in multidrug efflux homologs, sugar isomerases, and
RT antimicrobial biosynthesis genes differentially elevate activity of
RT the sigma(X) and sigma(W) factors in Bacillus subtilis.";
RL J. Bacteriol. 182:5202-5210(2000).
CC -!- CATALYTIC ACTIVITY: D-mannose 6-phosphate = D-fructose 6-
CC phosphate.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow
CC in minimal medium with mannose as a sole carbon source. They show
CC impaired growth in rich medium, and impairment increases in the
CC presence of greater than 1.4 mM mannose.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL009126; CAB13059.1; -; Genomic_DNA.
DR PIR; H69848; H69848.
DR RefSeq; NP_389084.1; NC_000964.3.
DR HSSP; P39841; 1QWR.
DR ProteinModelPortal; O31646; -.
DR SMR; O31646; 2-315.
DR STRING; 224308.BSU12020; -.
DR PaxDb; O31646; -.
DR EnsemblBacteria; CAB13059; CAB13059; BSU12020.
DR GeneID; 939393; -.
DR KEGG; bsu:BSU12020; -.
DR PATRIC; 18974133; VBIBacSub10457_1259.
DR GenoList; BSU12020; -.
DR eggNOG; COG1482; -.
DR HOGENOM; HOG000054245; -.
DR KO; K01809; -.
DR OMA; VIETQQS; -.
DR ProtClustDB; CLSK887088; -.
DR BioCyc; BSUB:BSU12020-MONOMER; -.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR001250; Man6P_Isoase-1.
DR InterPro; IPR014628; Man6P_isomerase_Firm_short.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin.
DR PANTHER; PTHR18964:SF1; PTHR18964:SF1; 1.
DR Pfam; PF01238; PMI_typeI; 1.
DR PIRSF; PIRSF036894; PMI_Firm_short; 1.
DR SUPFAM; SSF51182; RmlC_like_cupin; 1.
DR TIGRFAMs; TIGR00218; manA; 2.
DR PROSITE; PS00965; PMI_I_1; FALSE_NEG.
DR PROSITE; PS00966; PMI_I_2; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; Isomerase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1 315 Mannose-6-phosphate isomerase ManA.
FT /FTId=PRO_0000371314.
FT ACT_SITE 192 192 By similarity.
FT METAL 97 97 Zinc (By similarity).
FT METAL 110 110 Zinc (By similarity).
FT METAL 172 172 Zinc (By similarity).
SQ SEQUENCE 315 AA; 36003 MW; 6848958CF5545064 CRC64;
MTTEPLFFKP VFKERIWGGT ALADFGYTIP SQRTGECWAF AAHQNGQSVV QNGMYKGFTL
SELWEHHRHL FGQLEGDRFP LLTKILDADQ DLSVQVHPND EYANIHENGE LGKTECWYII
DCQKDAEIIY GHNATTKEEL TTMIERGEWD ELLRRVKVKP GDFFYVPSGT VHAIGKGILA
LETQQNSDTT YRLYDYDRKD AEGKLRELHL KKSIEVIEVP SIPERHTVHH EQIEDLLTTT
LIECAYFSVG KWNLSGSASL KQQKPFLLIS VIEGEGRMIS GEYVYPFKKG DHMLLPYGLG
EFKLEGYAEC IVSHL
//
