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Database: UniProt
Entry: G9YF61_9FIRM
LinkDB: G9YF61_9FIRM
Original site: G9YF61_9FIRM 
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
//
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