MANA1_BACSU
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 03-AUG-2022, entry version 123.
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; Firmicutes; 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; O31646; -.
DR PRIDE; O31646; -.
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 OMA; FRPKIWG; -.
DR PhylomeDB; O31646; -.
DR BioCyc; BSUB:BSU12020-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:InterPro.
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 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
