ID   MANA3_BACSU             Reviewed;         316 AA.
AC   P39841;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Putative mannose-6-phosphate isomerase YvyI;
DE            EC=5.3.1.8;
DE   AltName: Full=Phosphohexomutase;
DE   AltName: Full=Phosphomannose isomerase;
DE            Short=PMI;
GN   Name=yvyI; Synonyms=pmi; OrderedLocusNames=BSU35790;
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;
RX   PubMed=7934877; DOI=10.1111/j.1365-2958.1994.tb01040.x;
RA   Margot P., Maueel C., Karamata D.;
RT   "The gene of the N-acetylglucosaminidase, a Bacillus subtilis 168 cell wall
RT   hydrolase not involved in vegetative cell autolysis.";
RL   Mol. Microbiol. 12:535-545(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / AC327;
RX   PubMed=7581999; DOI=10.1099/13500872-141-10-2391;
RA   Rashid M.H., Mori M., Sekiguchi J.;
RT   "Glucosaminidase of Bacillus subtilis: cloning, regulation, primary
RT   structure and biochemical characterization.";
RL   Microbiology 141:2391-2404(1995).
RN   [3]
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   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC.
RG   Midwest center for structural genomics (MCSG);
RT   "Crystal structure analysis of the mannose 6-phosphate isomerase from
RT   Bacillus subtilis.";
RL   Submitted (JAN-2005) to the PDB data bank.
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;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; U02562; AAA67856.1; -; Genomic_DNA.
DR   EMBL; D45048; BAA08088.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15596.1; -; Genomic_DNA.
DR   PIR; A69680; A69680.
DR   RefSeq; NP_391460.1; NC_000964.3.
DR   RefSeq; WP_003244253.1; NZ_JNCM01000034.1.
DR   PDB; 1QWR; X-ray; 1.80 A; A/B=1-316.
DR   PDBsum; 1QWR; -.
DR   AlphaFoldDB; P39841; -.
DR   SMR; P39841; -.
DR   IntAct; P39841; 1.
DR   STRING; 224308.BSU35790; -.
DR   DrugBank; DB01942; Formic acid.
DR   jPOST; P39841; -.
DR   PaxDb; 224308-BSU35790; -.
DR   DNASU; 936815; -.
DR   EnsemblBacteria; CAB15596; CAB15596; BSU_35790.
DR   GeneID; 936815; -.
DR   KEGG; bsu:BSU35790; -.
DR   PATRIC; fig|224308.179.peg.3874; -.
DR   eggNOG; COG1482; Bacteria.
DR   InParanoid; P39841; -.
DR   OrthoDB; 9808275at2; -.
DR   PhylomeDB; P39841; -.
DR   BioCyc; BSUB:BSU35790-MONOMER; -.
DR   EvolutionaryTrace; P39841; -.
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   3D-structure; Carbohydrate metabolism; Isomerase; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..316
FT                   /note="Putative mannose-6-phosphate isomerase YvyI"
FT                   /id="PRO_0000194228"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000250|UniProtKB:P34948"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|Ref.4"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|Ref.4"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|Ref.4"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          11..14
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   HELIX           21..26
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          31..41
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   TURN            55..58
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   HELIX           61..67
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   HELIX           69..72
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          82..91
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   HELIX           101..107
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   TURN            108..110
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          116..123
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          128..133
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   HELIX           138..146
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   HELIX           150..153
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          154..158
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          164..167
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          173..175
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          177..187
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          192..195
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   HELIX           211..217
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          230..234
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          237..244
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          249..261
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          268..281
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          284..289
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          293..296
FT                   /evidence="ECO:0007829|PDB:1QWR"
FT   STRAND          303..315
FT                   /evidence="ECO:0007829|PDB:1QWR"
SQ   SEQUENCE   316 AA;  35428 MW;  21E6FF26E7CF922F CRC64;
     MTQSPIFLTP VFKEKIWGGT ALRDRFGYSI PSESTGECWA ISAHPKGPST VANGPYKGKT
     LIELWEEHRE VFGGVEGDRF PLLTKLLDVK EDTSIKVHPD DYYAGENEEG ELGKTECWYI
     IDCKENAEII YGHTARSKTE LVTMINSGDW EGLLRRIKIK PGDFYYVPSG TLHALCKGAL
     VLETQQNSDA TYRVYDYDRL DSNGSPRELH FAKAVNAATV PHVDGYIDES TESRKGITIK
     TFVQGEYFSV YKWDINGEAE MAQDESFLIC SVIEGSGLLK YEDKTCPLKK GDHFILPAQM
     PDFTIKGTCT LIVSHI
//