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Database: UniProt
Entry: A0A1H2WZQ8_9FLAO
LinkDB: A0A1H2WZQ8_9FLAO
Original site: A0A1H2WZQ8_9FLAO 
ID   A0A1H2WZQ8_9FLAO        Unreviewed;       764 AA.
AC   A0A1H2WZQ8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Allosteric NADP-dependent malic enzyme {ECO:0000313|EMBL:SDW86075.1};
GN   ORFNames=SAMN04487892_2517 {ECO:0000313|EMBL:SDW86075.1};
OS   Allomuricauda zhangzhouensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=1073328 {ECO:0000313|EMBL:SDW86075.1, ECO:0000313|Proteomes:UP000199592};
RN   [1] {ECO:0000313|Proteomes:UP000199592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25030 {ECO:0000313|Proteomes:UP000199592};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FNMY01000003; SDW86075.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2WZQ8; -.
DR   STRING; 1073328.SAMN05216294_1137; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000199592; Unassembled WGS sequence.
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}.
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   764 AA;  84350 MW;  C06858639E52F7FA CRC64;
     MSKERQRREA LLYHAKPQPG KIKIVPTKPY STQRDLALAY SPGVAEPCLE IEKNKDDVYK
     YTAKGNIVAV ISNGTAVLGL GNIGPEASKP VMEGKSLLFK IFADIDGIDI ELDTTDVERF
     IQTVKTIAPT FGGINLEDIK APEAFEIERR LKEELDIPVM HDDQHGTAII SAAALLNALE
     IANKKIDEVK IVVSGAGAAA VSCTRLYKAF GAKGENIVML DSKGVIRSDR DNLSVEKKEF
     ATDRKIDTLD EAMIGADVFI GLSIADIVTP EMLKTMAQDP IVFAMANPDP EIEYNLACST
     RKDIIMATGR SDHPNQVNNV LGFPFIFRGA LDVRATKINE DMKMAAVRAL ADLTRESVPE
     QVNIAYDATR LTFGRNYIIP KPFDPRLITK IPPAVAKAAM ESGVAKAPIQ DWEKYEEELY
     QRSGNDNKVV RLLHNRAKVN PKRVVFAEAE LLDVMKAAQI VHDEGIAQPI LLGNKDIIEH
     LKRELDFDAE VPIIDPRSDE FSEMRSKYAL KLWESRKRKG ETKYSARVNM GKRNYFGAMM
     LKEGDADGMI SGYSRAYPKV LRPVFEVLGR AKNVKNASTV NIMITERGPM FLADTSINID
     PSAEELAEIA QMTANVAKTF GFSPVMAMLS YANFGSSSHP NAQKVREAVQ ILHETNPELV
     VDGEIQTDFA LDDVLCTNNF PFSKISGKKV NTLIFPNLES ANITYKLLKG LHKADSIGPI
     MVGLTKAAHI LQLGASVDEM VNMAAVAVID AQEREKRRKA KTEQ
//
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