(data stored in SCRATCH zone)

SWISSPROT: MAO1_BACSU

ID   MAO1_BACSU              Reviewed;         439 AA.
AC   P54572;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   11-DEC-2019, entry version 138.
DE   RecName: Full=Probable NAD-dependent malic enzyme 1;
DE            Short=NAD-ME 1;
DE            EC=1.1.1.38;
GN   Name=yqkJ; OrderedLocusNames=BSU23550;
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=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 432-439.
RX   PubMed=8501064; DOI=10.1128/jb.175.11.3607-3617.1993;
RA   Smith K., Bayer M.E., Youngman P.;
RT   "Physical and functional characterization of the Bacillus subtilis spoIIM
RT   gene.";
RL   J. Bacteriol. 175:3607-3617(1993).
RN   [4]
RP   DISCUSSION OF FUNCTION.
RX   PubMed=10903309; DOI=10.1074/jbc.m001112200;
RA   Wei Y., Guffanti A.A., Ito M., Krulwich T.A.;
RT   "Bacillus subtilis YqkI is a novel malic/Na+-lactate antiporter that
RT   enhances growth on malate at low protonmotive force.";
RL   J. Biol. Chem. 275:30287-30292(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC         Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.38;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:16526; EC=1.1.1.38;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
CC   -!- CAUTION: PubMed:10903309 has predicted this protein to be a malolactic
CC       enzyme which would convert malate to lactate. {ECO:0000305}.
DR   EMBL; D84432; BAA12645.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14287.1; -; Genomic_DNA.
DR   EMBL; L06664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; C69967; C69967.
DR   RefSeq; NP_390236.1; NC_000964.3.
DR   RefSeq; WP_004398731.1; NZ_JNCM01000036.1.
DR   SMR; P54572; -.
DR   STRING; 224308.BSU23550; -.
DR   jPOST; P54572; -.
DR   PaxDb; P54572; -.
DR   PRIDE; P54572; -.
DR   EnsemblBacteria; CAB14287; CAB14287; BSU23550.
DR   GeneID; 938725; -.
DR   KEGG; bsu:BSU23550; -.
DR   PATRIC; fig|224308.179.peg.2567; -.
DR   eggNOG; COG0281; LUCA.
DR   HOGENOM; HOG000132447; -.
DR   InParanoid; P54572; -.
DR   KO; K00027; -.
DR   OMA; FMAYGVK; -.
DR   PhylomeDB; P54572; -.
DR   BioCyc; BSUB:BSU23550-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.10380; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
DR   PRODOM; P54572.
DR   SWISS-2DPAGE; P54572.
KW   Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..439
FT                   /note="Probable NAD-dependent malic enzyme 1"
FT                   /id="PRO_0000160208"
FT   DOMAIN          9..84
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   NP_BIND         149..156
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        112
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   METAL           209
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000250"
FT   METAL           210
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   BINDING         347
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   439 AA;  45890 MW;  2C6863E83CA86939 CRC64;
     MIAKHMIRTL MIETPSVPGN LGRVATAIGL LGGDIGEVET VKVGPNYTMR NITVQVENEE
     QLQEVIAAVQ ALGEGIRLHT VSDEVLSAHE GGKIQMKSKM PIRSLAELGR VYTPGVADVC
     RLIEKEPEKA SIYTTISNSV AIVTDGTAIL GLGNIGSVAG MPVMEGKAAL FDQLAGISGI
     PILLDTSDPE EIIKTVKHIS PGFSGILLED IGSPHCFEIE DRLKEELNIP VMHDDQHGTA
     VVTLAAAISA CRSAGVDLKE AKVGQIGLGA AGVAICRMFM AYGVNAVYGT DKSESAMNRL
     EQYGGQAVSS IEELMETCDI VIATTGVPGL IKPAFVRSGQ VILALSNPKP EIEPEAALQA
     GAAYAADGRS VNNVLGFPGI FRGALNAKST EINHDMLVAA AEAIAACTKQ GDVVPQPLDS
     KVHHAVAAAV EHAALTAVK
//

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