ID   MANA2_BACSU             Reviewed;         315 AA.
AC   O05511; Q797D7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Probable mannose-6-phosphate isomerase GmuF;
DE            EC=5.3.1.8;
DE   AltName: Full=Glucomannan utilization protein F;
DE   AltName: Full=Phosphohexomutase;
DE   AltName: Full=Phosphomannose isomerase;
DE            Short=PMI;
GN   Name=gmuF; Synonyms=ydhS; OrderedLocusNames=BSU05870;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA   Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA   Ogasawara N.;
RT   "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT   Bacillus subtilis chromosome.";
RL   Microbiology 143:1861-1866(1997).
RN   [2]
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   [3]
RP   INDUCTION, AND FUNCTION IN GLUCOMANNAN UTILIZATION.
RC   STRAIN=168;
RX   PubMed=18177310; DOI=10.1111/j.1574-6968.2007.01018.x;
RA   Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K.;
RT   "Glucomannan utilization operon of Bacillus subtilis.";
RL   FEMS Microbiol. Lett. 279:103-109(2008).
CC   -!- FUNCTION: Seems to be involved in the degradation of glucomannan.
CC       {ECO:0000269|PubMed:18177310}.
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 konjac glucomannan and by cellobiose and
CC       mannobiose, the possible degradation products of glucomannan. Repressed
CC       by glucose via the carbon catabolite repression system. Also repressed
CC       by GmuR. {ECO:0000269|PubMed:18177310}.
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; D88802; BAA19711.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12406.1; -; Genomic_DNA.
DR   PIR; G69785; G69785.
DR   RefSeq; NP_388468.1; NC_000964.3.
DR   RefSeq; WP_003242491.1; NZ_JNCM01000031.1.
DR   AlphaFoldDB; O05511; -.
DR   SMR; O05511; -.
DR   STRING; 224308.BSU05870; -.
DR   PaxDb; 224308-BSU05870; -.
DR   EnsemblBacteria; CAB12406; CAB12406; BSU_05870.
DR   GeneID; 938028; -.
DR   KEGG; bsu:BSU05870; -.
DR   PATRIC; fig|224308.179.peg.631; -.
DR   eggNOG; COG1482; Bacteria.
DR   InParanoid; O05511; -.
DR   OrthoDB; 9808275at2; -.
DR   PhylomeDB; O05511; -.
DR   BioCyc; BSUB:BSU05870-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:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Isomerase; Metal-binding; Reference proteome;
KW   Zinc.
FT   CHAIN           1..315
FT                   /note="Probable mannose-6-phosphate isomerase GmuF"
FT                   /id="PRO_0000372435"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000250|UniProtKB:P34948"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
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;  35492 MW;  ED6F1855D41B4DDF CRC64;
     MTHPLFLEPV FKERLWGGTK LRDAFGYAIP SQKTGECWAV SAHAHGSSSV KNGPLAGKTL
     DQVWKDHPEI FGFPDGKVFP LLVKLLDANM DLSVQVHPDD DYAKLHENGD LGKTECWYII
     DCKDDAELIL GHHASTKEEF KQRIESGDWN GLLRRIKIKP GDFFYVPSGT LHALCKGTLV
     LEIQQNSDTT YRVYDYDRCN DQGQKRTLHI EKAMEVITIP HIDKVHTPEV KEVGNAEIIV
     YVQSDYFSVY KWKISGRAAF PSYQTYLLGS VLSGSGRIIN NGIQYECNAG SHFILPAHFG
     EFTIEGTCEF MISHP
//