MANA3_BACSU
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 03-AUG-2022, entry version 142.
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; Firmicutes; 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; P39841; -.
DR PRIDE; P39841; -.
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 OMA; ITIKTFV; -.
DR PhylomeDB; P39841; -.
DR BioCyc; BSUB:BSU35790-MON; -.
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 GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
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_sf.
DR Pfam; PF01238; PMI_typeI; 1.
DR PIRSF; PIRSF036894; PMI_Firm_short; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR00218; manA; 2.
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
