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Database: UniProt
Entry: A0A2P7TC77_9SPHI
LinkDB: A0A2P7TC77_9SPHI
Original site: A0A2P7TC77_9SPHI 
ID   A0A2P7TC77_9SPHI        Unreviewed;       395 AA.
AC   A0A2P7TC77;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:PSJ72321.1};
GN   ORFNames=C7N43_34850 {ECO:0000313|EMBL:PSJ72321.1};
OS   Sphingobacteriales bacterium UPWRP_1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=2116516 {ECO:0000313|EMBL:PSJ72321.1, ECO:0000313|Proteomes:UP000240367};
RN   [1] {ECO:0000313|EMBL:PSJ72321.1, ECO:0000313|Proteomes:UP000240367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UPWRP_1 {ECO:0000313|EMBL:PSJ72321.1,
RC   ECO:0000313|Proteomes:UP000240367};
RA   Tan S.M.;
RT   "Obtaining draft genomes of rare unknown microbial groups and defining 1
RT   their spatial structures from highly complex communities.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|PIRSR:PIRSR000106-3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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:PSJ72321.1}.
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DR   EMBL; PXYE01000248; PSJ72321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P7TC77; -.
DR   Proteomes; UP000240367; Unassembled WGS sequence.
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   CDD; cd05311; NAD_bind_2_malic_enz; 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; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   PIRSF; PIRSF000106; ME; 1.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 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:PIRSR000106-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240367}.
FT   DOMAIN          16..149
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          160..389
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        37
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         134
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         135
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         159
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   395 AA;  41910 MW;  A7157CC8109B2402 CRC64;
     MDKISRESLL LHQQLGGKIS VSPKMDIENT RDLSLLYSPG VAEPCLQIAD NPDEVWKYTI
     KNNTVAVVSD GSAVLGLGNI GPLAAIPVME GKAMLFKKFA GIDAFPICLN TQDTDEIVQT
     VKNIAPVFGG INLEDISAPR CFEIEDRLQD IGIPVFHDDQ HGTAVVALAA LINACKVTGK
     KLEDLKVVIN GSGAAGVAIA RLLRCVSSNH EACIPVKSVL MADTKGIIHR NRTDLNGIKQ
     EVLRYTNPSD ETGSLRDALK NADVFIGVSV GNLLTPDDIR LMADNAIVFA LANPTPEIMP
     DKAFAGGAAI VGTGRSDFPN QINNVLGFPG IFRGALNARA KTITPYMKLA AAYAIANCVT
     KPTPQQIIPS VLDASVVKAV AKAVTIAAKQ ELVAL
//
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