ID A0A0D5YUI8_9FLAO Unreviewed; 765 AA.
AC A0A0D5YUI8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=NAD-binding malic protein {ECO:0000313|EMBL:AKA35544.1};
GN ORFNames=VC82_1939 {ECO:0000313|EMBL:AKA35544.1};
OS Allomuricauda lutaonensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=516051 {ECO:0000313|EMBL:AKA35544.1, ECO:0000313|Proteomes:UP000032726};
RN [1] {ECO:0000313|EMBL:AKA35544.1, ECO:0000313|Proteomes:UP000032726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-HSB-11 {ECO:0000313|EMBL:AKA35544.1,
RC ECO:0000313|Proteomes:UP000032726};
RA Kim K.M.;
RT "Complete genome sequence of Muricauda lutaonensis CC-HSB-11T, isolated
RT from a coastal hot spring.";
RL Submitted (MAR-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; CP011071; AKA35544.1; -; Genomic_DNA.
DR RefSeq; WP_045802190.1; NZ_CP011071.1.
DR AlphaFoldDB; A0A0D5YUI8; -.
DR STRING; 516051.VC82_1939; -.
DR KEGG; mlt:VC82_1939; -.
DR PATRIC; fig|516051.4.peg.1998; -.
DR HOGENOM; CLU_012366_0_0_10; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000032726; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000032726}.
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 765 AA; 84497 MW; 4B0196F5CD49DC0C CRC64;
MNKEKQRREA LVYHAKPQPG KIKVVPTKPY ATQRDLALAY SPGVAQPCLE IEKNKDEVYR
YTAKGNVVAV ISNGTAVLGL GNIGPEASKP VMEGKSLLFK IFADIDGIDI ELDTEDVDKF
VETVKTIAPT FGGINLEDIK APEAFEIERR LKEELDIPVM HDDQHGTAII SAAALLNALE
LAEKKIEEVT IVISGAGAAA VSCSRLYKAF GAKGENMVML DSKGVIRKDR ENLSKEKLEF
ATDRKIDTLE EAMKGADVFI GLSIADIVTP EMLKSMAKNP IVFAMANPNP EIEYELACKT
RDDIIMATGR SDHPNQVNNV LGFPFIFRGA LDVRATKINE AMKMAAVRAL ADLAKEPVPE
QVNITYDTTR LTFGKEYIIP KPFDPRLITK IPPAVAKAAI ESGVARIPIR DWKKYEEELY
LRSGNDNKIV RSLHNRAKVD PKHIVFAEAD VLDVLKAAQI VYDEGIAKPI LLGNKEIIKE
LKEELDFDAE VPIIDPRAEE TRELRKKYAY KLWQSRRRKG ETEYSAGVNM GKRNYFGSMM
LLEGDADGLI SGYSRAYPKV LRPVFEVLGK ASGVTKASTV NIMITKRGPL FLADTSVNVD
PTAEELAEIA QMTANLAKTF GFEPVVALLS YANFGSSSHP HAKKVRDAVK ILHEKNPDLV
VDGEIQTDFA LNQELCQNNF PFSKLAGRKA NTLIFPNLES ANITYKLLKG LHDAESIGPI
MLGLRKAAHI LQLGASVEEM VNMAAVAVID AQEREKRKKA RMKKG
//
