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   27-MAR-2024, entry version 131.
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; Bacillota; 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., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., 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., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., 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; DOI=10.1099/00221287-145-12-3419;
RA   Reizer J., Bachem S., Reizer A., Arnaud M., Saier M.H. Jr., Stuelke J.;
RT   "Novel phosphotransferase system genes revealed by genome analysis - the
RT   complete complement of PTS proteins encoded within the genome of Bacillus
RT   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 the
RT   sigma(X) and sigma(W) factors in Bacillus subtilis.";
RL   J. Bacteriol. 182:5202-5210(2000).
RN   [4]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20139185; DOI=10.1128/jb.01673-09;
RA   Sun T., Altenbuchner J.;
RT   "Characterization of a mannose utilization system in Bacillus subtilis.";
RL   J. Bacteriol. 192:2128-2139(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate;
CC         Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527;
CC         EC=5.3.1.8;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- INDUCTION: Up-regulated by mannose. Is under the control of ManR. Is
CC       subject to carbon catabolite repression (CCR) by glucose. Forms part of
CC       an operon with manP and yjdF. {ECO:0000269|PubMed:20139185}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow in
CC       minimal medium with mannose as the 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. {ECO:0000269|PubMed:10960106,
CC       ECO:0000269|PubMed:20139185}.
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AL009126; CAB13059.1; -; Genomic_DNA.
DR   PIR; H69848; H69848.
DR   RefSeq; NP_389084.1; NC_000964.3.
DR   RefSeq; WP_003232833.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O31646; -.
DR   SMR; O31646; -.
DR   STRING; 224308.BSU12020; -.
DR   jPOST; O31646; -.
DR   PaxDb; 224308-BSU12020; -.
DR   EnsemblBacteria; CAB13059; CAB13059; BSU_12020.
DR   GeneID; 939393; -.
DR   KEGG; bsu:BSU12020; -.
DR   PATRIC; fig|224308.179.peg.1297; -.
DR   eggNOG; COG1482; Bacteria.
DR   InParanoid; O31646; -.
DR   OrthoDB; 9808275at2; -.
DR   PhylomeDB; O31646; -.
DR   BioCyc; BSUB:BSU12020-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd07010; cupin_PMI_type_I_N_bac; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR001250; Man6P_Isoase-1.
DR   InterPro; IPR014628; Man6P_isomerase_Firm_short.
DR   InterPro; IPR049071; MPI_cupin_dom.
DR   InterPro; IPR046457; PMI_typeI_cat.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   NCBIfam; TIGR00218; manA; 2.
DR   PANTHER; PTHR42742:SF3; MANNOSE-6-PHOSPHATE ISOMERASE GMUF-RELATED; 1.
DR   PANTHER; PTHR42742; TRANSCRIPTIONAL REPRESSOR MPRA; 1.
DR   Pfam; PF21621; MPI_cupin_dom; 1.
DR   Pfam; PF20511; PMI_typeI_cat; 1.
DR   PIRSF; PIRSF036894; PMI_Firm_short; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   2: Evidence at transcript level;
KW   Isomerase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..315
FT                   /note="Mannose-6-phosphate isomerase ManA"
FT                   /id="PRO_0000371314"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000250|UniProtKB:P34948"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P39841"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P39841"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P39841"
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
//