ID A0A0F4KQE2_9LACO Unreviewed; 542 AA.
AC A0A0F4KQE2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Malolactic enzyme {ECO:0000313|EMBL:KJY48278.1};
GN Name=mleS {ECO:0000313|EMBL:KJY48278.1};
GN ORFNames=JG29_13300 {ECO:0000313|EMBL:KJY48278.1};
OS Bombilactobacillus mellis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Bombilactobacillus.
OX NCBI_TaxID=1218508 {ECO:0000313|EMBL:KJY48278.1, ECO:0000313|Proteomes:UP000033695};
RN [1] {ECO:0000313|EMBL:KJY48278.1, ECO:0000313|Proteomes:UP000033695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hon2 {ECO:0000313|EMBL:KJY48278.1,
RC ECO:0000313|Proteomes:UP000033695};
RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA Vasquez A.;
RT "Comparative genomics of the lactic acid bacteria isolated from the honey
RT bee gut.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJY48278.1}.
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; JXBZ01000009; KJY48278.1; -; Genomic_DNA.
DR RefSeq; WP_045923167.1; NZ_KQ033878.1.
DR AlphaFoldDB; A0A0F4KQE2; -.
DR STRING; 1218508.JG29_13300; -.
DR PATRIC; fig|1218508.4.peg.1320; -.
DR HOGENOM; CLU_011405_5_2_9; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000033695; Unassembled WGS sequence.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0043883; F:malolactic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0043464; P:malolactic fermentation; IEA:InterPro.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
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; IPR048182; Malolactic_enz.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; NF041582; malolactic; 1.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000033695}.
FT DOMAIN 69..251
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 261..517
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 92
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 236
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 237
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 260
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 542 AA; 59347 MW; 17B0FC778BC159E7 CRC64;
MTKTGQDVLN DPFLNHGTGF TSTERKTLHL QGLLPPQVQT IDQQAQIAYE QVQGKNSNLE
KRLFLMTLFN TNRTLFFYLF RQHLPEFMPL VYDPTIAETI ENYSHLFINP QQAAFLSIKH
QDEMAETLKT AAAGRSIKLI VVTDGEAILG IGDWGTQGVD IAIGKLMVYT AAAGLNPAQV
LPVVLDAGTN NPTLLQDSFY LGLHQQRIQG EPYYQFVDNF VQTAEQLFPN MYLHFEDFGR
DNAAAILNHY QDQFLTFNDD IQGTGIIVLS AILGALKISQ QKLTEQKYLC FGAGTAGMGI
VKQIYHEMIQ EGLSPTAAQK RFYLVDKQGL LFDDTAALTP EQKPFTRSRK EFAHSDSLTT
LKAAVTAIQP TILVGTSTQA GAFDEDIVQA MSRYTPRPII FPLSNPTKLA EATAADLIRW
SHGRALVATG IPSAPVDYQG ISYQIGQANN ALVYPGLGMG AIAAQAKILS TNMISAAAHS
LGEMVDFRQP GAAVLPPISQ LELFSQTIAE NVCNQAIKDG LSQNNCPNGA EAVATIKWSA
HY
//
