ID A0A0C1FT86_9FLAO Unreviewed; 763 AA.
AC A0A0C1FT86;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:KIA96112.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:KIA96112.1};
GN ORFNames=OA93_17545 {ECO:0000313|EMBL:KIA96112.1};
OS Flavobacterium sp. KMS.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1566023 {ECO:0000313|EMBL:KIA96112.1, ECO:0000313|Proteomes:UP000031466};
RN [1] {ECO:0000313|EMBL:KIA96112.1, ECO:0000313|Proteomes:UP000031466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:KIA96112.1,
RC ECO:0000313|Proteomes:UP000031466};
RA Smith A.K., Newman J.;
RT "Flavobacterium sp. KMS.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KIA96112.1}.
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DR EMBL; JSYP01000018; KIA96112.1; -; Genomic_DNA.
DR RefSeq; WP_039114890.1; NZ_JSYP01000018.1.
DR AlphaFoldDB; A0A0C1FT86; -.
DR STRING; 1566023.OA93_17545; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000031466; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase 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:KIA96112.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031466}.
FT DOMAIN 19..152
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 164..400
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 77..84
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 163
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; 83324 MW; 0A642C84B5AF346E CRC64;
MNKDSKRSEA LLYHSKPTPG KIQVVPTKKY ATQRDLSLAY SPGVAEPCLE IARDVNEVYK
YTAKGNLVAV ITNGTAVLGL GDIGPEASKP VMEGKGLLFK IFSDIDVFDI EIGTKDIEEF
IQTVKNIAPT FGGINLEDIK APESFEIERR LVEELNIPVM HDDQHGTAII SSAALINALE
LADKKAEDVK MVVSGAGSAA LACADLYVLL GVKIENILMY NSKGLLTKNN PALSALQLKY
AKDIEPIGLE EALKGADIFL GLSSGDIMTA DMLLGMAENP IVFAMANPDP EINYNLAITT
RKDVIMATGR SDYPNQVNNV LGFPYIFRGA LDVRATKINE AMKMAAVRAL ASLAKESVPE
QVNVAYGATK LGFGREYIIP KPFDPRLITV VAPAVAKAAM ESGVALNPIT DWEKYEEELL
ARLGNDNKMV RLITNRAKMD PKRIVFAEAD HLNVLKAAQI VYEEGIGFPI LLGNKEIILE
LKAELGFDAD VEIIDPKTKD QEERRNQFAS SYWSTRERRG ISLLDAQKLM RERNYFAAMM
VNEGEADALV TGHSRSYPSV VKPMLQLIEK APGASLVATA NMMMTNRGPM FLSDTAININ
PSADDLAKIA VMTAKTAKMF GVEPVIAMVS YSNFGSSTNP GAAKVREAVA YLHKNHPELV
IDGEIQADFA LNPEMLQEKF PFSKLAGKKV NTLIFPNLES ANITYKLLKE LNKVDSIGPI
MLGMGKPVHI FQLGASVEEM VNMAAIAVID AQEKEIKKNN LIK
//
