ID A8FID4_BACP2 Unreviewed; 566 AA. AC A8FID4; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 04-NOV-2026, entry version 108. DE RecName: Full=Malolactic enzyme {ECO:0000256|ARBA:ARBA00074565}; DE EC=4.1.1.101 {ECO:0000256|ARBA:ARBA00066983}; GN OrderedLocusNames=BPUM_3348 {ECO:0000313|EMBL:ABV64001.1}; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV64001.1, ECO:0000313|Proteomes:UP000001355}; RN [1] {ECO:0000313|EMBL:ABV64001.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV64001.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y., RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., RA Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). RN [2] {ECO:0000313|EMBL:ABV64001.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV64001.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=23812891; DOI=10.1007/s00792-013-0559-z; RA Tirumalai M.R., Fox G.E.; RT "An ICEBs1-like element may be associated with the extreme radiation and RT desiccation resistance of Bacillus pumilus SAFR-032 spores."; RL Extremophiles 17:767-774(2013). RN [3] {ECO:0000313|EMBL:ABV64001.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV64001.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=23799069; RA Tirumalai M.R., Rastogi R., Zamani N., O'Bryant Williams E., Allen S., RA Diouf F., Kwende S., Weinstock G.M., Venkateswaran K.J., Fox G.E.; RT "Candidate genes that may be responsible for the unusual resistances RT exhibited by Bacillus pumilus SAFR-032 spores."; RL PLoS ONE 8:E66012-E66012(2013). CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate + H(+) = (S)-lactate + CO2; Xref=Rhea:RHEA:46276, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16651; EC=4.1.1.101; CC Evidence={ECO:0000256|ARBA:ARBA00051739}; 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 -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000256|ARBA:ARBA00001911}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the malic enzymes family. CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}. 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; CP000813; ABV64001.1; -; Genomic_DNA. DR RefSeq; WP_012011565.1; NC_009848.4. DR AlphaFoldDB; A8FID4; -. DR STRING; 315750.BPUM_3348; -. DR PaxDb; 315750-BPUM_3348; -. DR GeneID; 5622638; -. DR KEGG; bpu:BPUM_3348; -. DR eggNOG; COG0281; Bacteria. DR HOGENOM; CLU_011405_5_2_9; -. DR OMA; AADRFWF; -. DR OrthoDB; 3314528at2; -. DR Proteomes; UP000001355; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro. DR GO; GO:0043883; F:malolactic enzyme activity; IEA:UniProtKB-EC. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-ARBA. 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:L-malate catabolic process; IEA:UniProtKB-ARBA. DR CDD; cd05312; NAD_bind_1_malic_enz; 1. DR FunFam; 3.40.50.10380:FF:000001; NAD-dependent malic enzyme; 1. DR FunFam; 3.40.50.720:FF:000182; NAD-dependent malic enzyme; 1. 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; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; NF010052; maeA; 1. DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1. DR PANTHER; PTHR23406:SF34; 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 Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000106-3}; NAD {ECO:0000256|ARBA:ARBA00023027}; KW Oxidoreductase {ECO:0000313|EMBL:ABV64001.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001355}. FT DOMAIN 82..264 FT /note="Malic enzyme N-terminal" FT /evidence="ECO:0000259|SMART:SM01274" FT DOMAIN 274..535 FT /note="Malic enzyme NAD-binding" FT /evidence="ECO:0000259|SMART:SM00919" FT ACT_SITE 105 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1" FT ACT_SITE 178 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1" FT BINDING 249 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3" FT BINDING 250 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3" FT BINDING 273 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3" FT BINDING 423 FT /ligand="(S)-malate" FT /ligand_id="ChEBI:CHEBI:15589" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2" FT BINDING 467 FT /ligand="(S)-malate" FT /ligand_id="ChEBI:CHEBI:15589" FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2" SQ SEQUENCE 566 AA; 62364 MW; 3C1B840BB4105E43 CRC64; MNNVKKTKEG YLETTLTGKD VLSIPTLNKG VAFSEEERQE LGLEGLLPPT VLTLEQQAER AYKQFLAQPD RLRQNVYLSD LQNRNEVLFY KLISDKLREM LPVVYTPTVG EAIQEYSHEY RRPHGVYLSI DNIDGIEKAF ENLHATAGDI DLIVATDSES ILGIGDWGVG GINIAIGKLA VYTAAAGIDP SRVIPVVLDV GTNNEKLLND PLYIGNHHKR VQGEKYEEFI DAYVKAALKF FPKALLHWED LGNKNARNIM KKYNDNILTF NDDIQGTGAI TLAGVLAAVK KTGTQLKDHR VMIFGAGSAG IGIADQMRDT MVLEGLTEEE ANNAFWTLDY RGLLTDQFED EVFDFQKPYL RSSDEVEGWA RDEKGQISFA EAVRQVKPTI LIGTSGQGGA FTEEIIKEIA AHTERPVIMP MSNPTPLAEA VPEDLFKWTD GRALVATGSP FENVEYNGIE HEIGQSNNAF VFPGLGLGSI VTESKIITKG MFVASADAIA EMVDHDKPGA GLLPSIDKLQ EVSIKVAIEV AKAAIKDGVA RKTPDDIEQA VKDAMWIPEY KKIVRA //