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Database: UniProt
Entry: V7I6D2_9CLOT
LinkDB: V7I6D2_9CLOT
Original site: V7I6D2_9CLOT 
ID   V7I6D2_9CLOT            Unreviewed;       392 AA.
AC   V7I6D2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:ETA80754.1};
GN   ORFNames=T472_0210125 {ECO:0000313|EMBL:ETA80754.1};
OS   Youngiibacter fragilis 232.1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Youngiibacter.
OX   NCBI_TaxID=994573 {ECO:0000313|EMBL:ETA80754.1, ECO:0000313|Proteomes:UP000017747};
RN   [1] {ECO:0000313|EMBL:ETA80754.1, ECO:0000313|Proteomes:UP000017747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=232.1 {ECO:0000313|EMBL:ETA80754.1,
RC   ECO:0000313|Proteomes:UP000017747};
RX   PubMed=24459265;
RA   Wawrik C.B., Callaghan A.V., Stamps B.W., Wawrik B.;
RT   "Genome Sequence of Youngiibacter fragilis, the Type Strain of the Genus
RT   Youngiibacter.";
RL   Genome Announc. 2:e01183-13(2014).
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:ETA80754.1}.
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DR   EMBL; AXUN02000173; ETA80754.1; -; Genomic_DNA.
DR   RefSeq; WP_023387113.1; NZ_AXUN02000173.1.
DR   AlphaFoldDB; V7I6D2; -.
DR   STRING; 994573.T472_0210125; -.
DR   PATRIC; fig|994573.3.peg.1885; -.
DR   eggNOG; COG0281; Bacteria.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000017747; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd05311; NAD_bind_2_malic_enz; 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; IPR045213; Malic_NAD-bd_bact_type.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR   PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 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:UP000017747}.
FT   DOMAIN          16..149
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          161..385
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        37
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         134
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         135
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         160
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   392 AA;  42219 MW;  D11C5C22C413C60F CRC64;
     MKSIYEVALE KHAEWKGKLT VELKTPLESK EDLSIAYTPG VAQPCLEIAK NKDDAFKYTW
     KGNIVAVVSD GTAVLGLGDI GPEAALPVME GKAVLFKRFG GVNAIPIVLD TKDPDEIINI
     VKKMAPTFGG INLEDISAPR CVQIERKLIE ELDIPVFHDD QHGTAIVVTA GLINALKIVK
     KKPEEITAVV SGAGAAGSSI IKMLKAFGVA NIYAFNSKGV IHRDDMEKYN FVVQEIAMMT
     NNDNKKLTLA EAMAESDLFI GVSAPKIITK EMVASMKKDA IVFAMANPEP EIGYHDAKEA
     GARVVGTGRS DFPNQVNNVL AFPGLFRGAL DVRSRKITDE MKMAAAEGIA ALIAEADITE
     EYVIPSPFDP RVAEAVAKAV SEKAIEQGLA RL
//
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