ID F8DF37_STREP Unreviewed; 540 AA.
AC F8DF37;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Putative NAD-dependent malic enzyme 3 {ECO:0000313|EMBL:AEH55110.1};
DE EC=1.1.1.38 {ECO:0000313|EMBL:AEH55110.1};
GN OrderedLocusNames=HMPREF0833_10079 {ECO:0000313|EMBL:AEH55110.1};
OS Streptococcus parasanguinis (strain ATCC 15912 / DSM 6778 / CIP 104372 /
OS LMG 14537).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=760570 {ECO:0000313|EMBL:AEH55110.1, ECO:0000313|Proteomes:UP000001502};
RN [1] {ECO:0000313|Proteomes:UP000001502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15912 / DSM 6778 / CIP 104372 / LMG 14537
RC {ECO:0000313|Proteomes:UP000001502};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RT "Complete sequence of Streptococcus parasanguinis strain ATCC 15912.";
RL Submitted (JUN-2011) 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}.
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DR EMBL; CP002843; AEH55110.1; -; Genomic_DNA.
DR RefSeq; WP_003017582.1; NC_015678.1.
DR AlphaFoldDB; F8DF37; -.
DR GeneID; 75174991; -.
DR KEGG; scp:HMPREF0833_10079; -.
DR HOGENOM; CLU_011405_5_2_9; -.
DR Proteomes; UP000001502; Chromosome.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
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:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:AEH55110.1}.
FT DOMAIN 67..249
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 259..515
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 234
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 258
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 540 AA; 59603 MW; 1A8497EECBED70A1 CRC64;
MKSHEILNNP FLNKGTAFTM EERKELGLIG LLPPYVQTIE EQAEQAYQHF LRKPSDLEKR
LFLMEIFNTN RTLFYYLFNQ HIVEFNPIVY DPVIADTIEQ YSELFVDPQY AAYLDINHPE
NIEETLKNAA GDRDIRLIVA TDAEGILGIG DWGVQGVDIS VGKLMVYTAA AGIDPACVMP
LVIDAGTNRE ELLNNPMYLG NRHERVRGEK YDAFIDQFVQ TAGKLFPKLY LHWEDFGRSN
AADILNRYKK EIPTFNDDIQ GTGIVVLGGI FGAMDITGEK LTDQVYLCYG GGSAGAGIAD
RVHAEMVAEG LSPEEAYKRF FMIDKQGLLF DDMEDLTPAQ KPFAKKRSDF EGKGDMTNLL
EVIKTVKPTI LVGTSTNPGA FTKEVVEAMC ENTERPVIFP ISNPTKKLEA TAQQVIEWSD
GKAFVATGVP SGTISYKGVD YEIGQANNAL IYPGLGLGML ASEAKLLTDE MIGAAAHSLS
GIVNPGQPGA PVLPPFQYVA DVSIKVAEAV AKKAQEQGLA QAKETDMAKA VRDLKWYPKY
//
