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Database: UniProt
Entry: D4VQV4_9BACE
LinkDB: D4VQV4_9BACE
Original site: D4VQV4_9BACE 
ID   D4VQV4_9BACE            Unreviewed;       763 AA.
AC   D4VQV4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:CDM04453.1};
DE            EC=1.1.1.40 {ECO:0000313|EMBL:CDM04453.1};
GN   ORFNames=BN890_20280 {ECO:0000313|EMBL:CDM04453.1};
OS   Bacteroides xylanisolvens SD CC 1b.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=702447 {ECO:0000313|EMBL:CDM04453.1, ECO:0000313|Proteomes:UP000019380};
RN   [1] {ECO:0000313|EMBL:CDM04453.1, ECO:0000313|Proteomes:UP000019380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ramaraj T., Sundararajan A., Mudge J., Schilkey F.D., Delvecchio V.,
RA   Donlon M., Ziemer C.;
RT   "Improved hybrid genome assemblies of Bacteroides xylanisolvens SD CC 1b
RT   and Bacteroides xylanisolvens SD CC 2a using Illumina and 454 Sequencing.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC       family. {ECO:0000256|ARBA:ARBA00007686}.
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:CDM04453.1}.
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DR   EMBL; CBXG010000020; CDM04453.1; -; Genomic_DNA.
DR   RefSeq; WP_004317276.1; NZ_ADKP01000201.1.
DR   AlphaFoldDB; D4VQV4; -.
DR   GeneID; 69481386; -.
DR   Proteomes; UP000019380; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
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:0006108; P:malate metabolic process; IEA:InterPro.
DR   CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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; 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; IPR012188; ME_PTA.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR042113; P_AcTrfase_dom1.
DR   InterPro; IPR042112; P_AcTrfase_dom2.
DR   InterPro; IPR002505; PTA_PTB.
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   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF036684; ME_PTA; 1.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036684-2};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW   Oxidoreductase {ECO:0000313|EMBL:CDM04453.1}.
FT   DOMAIN          18..151
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          163..400
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         76..83
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         136
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         137
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         162
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         287
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ   SEQUENCE   763 AA;  84023 MW;  1A41BEE412420945 CRC64;
     MAKITKEAAL LYHSQGKPGK IEVVPTKPYS TQTDLSLAYS PGVAEPCLEI EKNPQDAYKY
     TAKGNLVAVI SNGTAVLGLG DIGALSGKPV MEGKGLLFKI YAGIDVFDIE VDEKDPEKFI
     AAVKAIAPTF GGINLEDIKA PECFEIERRL KEELDIPVMH DDQHGTAIIS SAGLVNALQV
     AGKKIEDVKI VVNGAGASAV SCTKLYVSLG ARLENIVMLD SKGVISKTRT DLNEQKRYFA
     TDRTDIHTLE EAIKGADVFL GLSKGNVLSQ DMVRSMAPMP IVFALANPTP EISYEDAMAA
     RPDVLMATGR SDYPNQINNV IGFPYIFRGA LDTQAKAINE EMKIAAVHAI ANLAKQPVPD
     VVNAAYHVNN LSFGAEYFIP KPVDPRLITE VSCAVAKAAM ESGVARTEIK DWDAYCVHLR
     ELMGYESKLT RQLYDTARRS PQRVVFAEGI HPNMLKAAVE AKAEGICHPI LLGNDEAIGK
     LAEEMELSLE GIEIVNLRHP DESDRRERYS RILAEKRARE GFTYEEANDK MFERNYFGMM
     MVETGDADAF ITGLYTRYSN TIKVAKEVIG IQPGFKHFGT MHILNSKKGT YFLADTLINR
     HPDTETLIDI AKLSDKTVRF FNHTPVISML SYSNFGADTA GSPVKVHEAV AHMQEEYPEL
     AIDGEMQVNF AMNRELRDTK YPFTRLKGKD VNTLIFPNLS SANAGYKLLQ AMDPDTEFIG
     PIQMGLNKPI HFTDFESSVR DIVNITAVAV IDAIVDKKKR GVK
//
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