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
//