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Database: UniProt
Entry: G1W9L7_9BACT
LinkDB: G1W9L7_9BACT
Original site: G1W9L7_9BACT 
ID   G1W9L7_9BACT            Unreviewed;       761 AA.
AC   G1W9L7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=NADP-dependent malic enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF9431_00518 {ECO:0000313|EMBL:EGV34339.1};
OS   Segatella oulorum F0390.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=702438 {ECO:0000313|EMBL:EGV34339.1, ECO:0000313|Proteomes:UP000005141};
RN   [1] {ECO:0000313|EMBL:EGV34339.1, ECO:0000313|Proteomes:UP000005141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0390 {ECO:0000313|EMBL:EGV34339.1,
RC   ECO:0000313|Proteomes:UP000005141};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA   Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella oulorum F0390.";
RL   Submitted (JUL-2011) 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}.
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:EGV34339.1}.
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DR   EMBL; ADGI01000017; EGV34339.1; -; Genomic_DNA.
DR   RefSeq; WP_004379509.1; NZ_JH114215.1.
DR   AlphaFoldDB; G1W9L7; -.
DR   PATRIC; fig|702438.4.peg.533; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0281; Bacteria.
DR   HOGENOM; CLU_012366_0_0_10; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000005141; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005141}.
FT   DOMAIN          18..151
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          163..400
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         76..83
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         136
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         137
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         162
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   761 AA;  83759 MW;  A4002A79EF6A35D7 CRC64;
     MVKITKEAAL EYHSNGRPGK IEVKPTKPYS TQTDLSLAYS PGVAFPCLEI QATPDDAYKY
     TDKGNLVAVI SNGTAVLGLG DIGAMSGKPV MEGKGLLFKI YGGIDVFDIE VAEKDPEKFC
     EAVEKIAPTF GGINLEDIKA PECFYIEERL KKTLDIPVMH DDQHGTAIIS AAGLLNALEV
     AGKKIEDVKI VVNGAGAAAI SCTKLYVALG ARLENIVMLD SHGVINTERK DLNEQKKQFA
     THRTDAHTLE EAIKGADVFL GLSKGNILTQ DMVRSMAKNP IVFALANPVP EISYEDALAS
     RPDVLMSTGR SDYPNQINNV IGFPYIFRGA LDVHAKAINE AMKLAAVKAI AELAKQPVPD
     VVNEVYRVTD LTFGPKYFIP KPVDPRLITE VSAAVAKAAI ESGVARTTIT DWEAYKQNLR
     QLLGQETALT RKLHDTARLH PQRVVFAEGG HATMMKAAVQ AKQEGICEPI LLGNPDRLNR
     LAARLKLDLT GVEIIDMRAD QEQGRRATFA KQLAERRARQ GYTFEEAYDK MYERNYFGMS
     LVENGYADAF ITGLYTKYSN TIKVAKEVIG IKDGYNTFAT MHILNTKKGV YYVADTLINR
     HPDAEVLTDI AKLSKQTVEF FNEEPVIAML SYSNFGSDEV GSPTRVHQAV KQMQNEFPNL
     AIDGEMQVNF ALDKTLRDDK FPFSRLKGKE VNTLVFPNMS SANCSYKLLQ ALNPDCEIIG
     PIQMGLNRAI HFTDFESSVQ DVVNITAVAV IDAYVEKLKK A
//
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