MANA2_BACSU
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 03-AUG-2022, entry version 119.
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; Firmicutes; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; O05511; -.
DR PRIDE; O05511; -.
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 OMA; DYDRCND; -.
DR PhylomeDB; O05511; -.
DR BioCyc; BSUB:BSU05870-MON; -.
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 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
