ID G9YF61_9FIRM Unreviewed; 545 AA.
AC G9YF61;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Putative NAD-dependent malic enzyme 3 {ECO:0000313|EMBL:EHM43396.1};
GN ORFNames=HMPREF0080_00271 {ECO:0000313|EMBL:EHM43396.1};
OS Anaeroglobus geminatus F0357.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Anaeroglobus.
OX NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM43396.1, ECO:0000313|Proteomes:UP000005481};
RN [1] {ECO:0000313|EMBL:EHM43396.1, ECO:0000313|Proteomes:UP000005481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0357 {ECO:0000313|EMBL:EHM43396.1,
RC ECO:0000313|Proteomes:UP000005481};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-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}.
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:EHM43396.1}.
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DR EMBL; AGCJ01000009; EHM43396.1; -; Genomic_DNA.
DR RefSeq; WP_006789256.1; NZ_JH417567.1.
DR AlphaFoldDB; G9YF61; -.
DR STRING; 861450.HMPREF0080_00271; -.
DR PATRIC; fig|861450.3.peg.258; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_9; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000005481; Unassembled WGS sequence.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) 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: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: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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000005481}.
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 545 AA; 60172 MW; 0CD616F496779357 CRC64;
MKKTGYDLLN DPFLNKGTAF TDEERKEYGL VGLLPPRVQS LEEQAQQAYE HICRKDAGIE
KRRFLMQLFD TNRTLFYKVF SEHVAEFMPV VYDPVIAENI EEYSELFVNP QNAVFLSIDR
PEDIEESLKS GAAGRDIRLV VVSDAEEILG IGDWGTNGVD ISVGKLMVYT AAAGVNPEQV
LPVILDCGTN RKALLDDSLY LGNRHERVTG EKYYDFLQSF VETVERLFPK LYLHFEDFGR
DHAAALLQKY NKIYPVFNDD IQGTGIITLA GILGGLEISK EKLIDQVYMC FGAGTAGCGI
ARRVYSEMVA QGLSPEEAKK HFYLVDRQGL LFDDTPGLTP EQKEFTRKRE EFVNSHELTT
LEAAVKAVNP TVLVGTSTVP GAFTESIVRH MADTTKRPFI FPLSNPTKLA EAKAENLIEW
TDGRGLVATG IPAAPVMYKG IMYYIGQANN ALIYPGLGLG VLASEAKLLT DEMISAAAHS
LGGIIDTTQP GAATLPPVDK LTEFSHTVAV AVAKEAVRTG QSKFSEAEAL HNVDTLKWFP
EEVVP
//