ID A0A0P0CNE9_9FLAO Unreviewed; 763 AA.
AC A0A0P0CNE9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:ALJ05988.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:ALJ05988.1};
GN ORFNames=APS56_12975 {ECO:0000313|EMBL:ALJ05988.1};
OS Pseudalgibacter alginicilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pseudalgibacter.
OX NCBI_TaxID=1736674 {ECO:0000313|EMBL:ALJ05988.1, ECO:0000313|Proteomes:UP000057981};
RN [1] {ECO:0000313|EMBL:ALJ05988.1, ECO:0000313|Proteomes:UP000057981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ-22 {ECO:0000313|Proteomes:UP000057981};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; CP012898; ALJ05988.1; -; Genomic_DNA.
DR RefSeq; WP_054729013.1; NZ_CP012898.1.
DR AlphaFoldDB; A0A0P0CNE9; -.
DR STRING; 1736674.APS56_12975; -.
DR KEGG; ahz:APS56_12975; -.
DR PATRIC; fig|1736674.3.peg.2653; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000057981; Chromosome.
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; 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; 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.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036684-2};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW Oxidoreductase {ECO:0000313|EMBL:ALJ05988.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000057981}.
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; 84347 MW; B1B5F0C2399B3785 CRC64;
MSKQSKRIEA LIYHAKPTPG KIKVVPTKKY ATQRDLSLAY SPGVAEPCLE IEKDVNNAYK
YTAKGNLVAV ISNGTAVLGL GNIGALAGKP VMEGKGLLFK IFADIDVFDI EVDTENVEEF
IATVKNIAPT FGGINLEDIK APEAFEIERR LKEELDIPVM HDDQHGTAII SAAALLNAVE
ITKKKIDEVK IVISGAGAAA ISCSRLYQAC GAKRENMVML DSKGVIRKDR ENLTSEKAEF
ATDRKIDTLD EAMLDADVFI GLSMADIVTP AMLLSMAKDP IVFAMANPNP EVDYDLAVAT
RKDIIMATGR SDHPNQVNNV LGFPFIFRGA LDVRATKINE AMKMAAVKAL ARLAKETVPE
QVNIAYGETR LVFGKEYIIP KPFDPRLIAE VPPAVAKAAM DSGVAKEPIL DWEKYKDTLL
ERLGSDNKMV RMLLNRAKIN PKRVVYAEAD HLKVLKAAQI AYEEGIAFPI LLGRKDVIQR
LMAEIEFDAD VPIIDPKSDE ENERKNKYAK VYWQQRKRRG ITYYSAQRLM RERNYFAAMM
VNEGDADALI SGYSRSYPTV VKPMLELVGM AKGITRVATT NLMMTKRGPL FLSDTSINID
PDSKDLAIIA QMTSEVVRMF GLEPVIAMTS YSNFGSSQSP RATKVREAVA SLHRHFPDMV
VDGELQTDFA LNSEMLSDKF PFSKLAGKKV NTLVFPNLDT ANITYKLLKE LNEAESIGPI
MMGMNKPVHI LQMDASVDEI VNMTAIAVID AQQKQIENNK AIK
//
