ID A0A0E9N536_9BACT Unreviewed; 780 AA.
AC A0A0E9N536;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=NADP-dependent malate dehydrogenase {ECO:0000313|EMBL:GAO44811.1};
GN Name=maeB {ECO:0000313|EMBL:GAO44811.1};
GN ORFNames=FPE01S_04_00540 {ECO:0000313|EMBL:GAO44811.1};
OS Flavihumibacter petaseus NBRC 106054.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1220578 {ECO:0000313|EMBL:GAO44811.1, ECO:0000313|Proteomes:UP000033121};
RN [1] {ECO:0000313|EMBL:GAO44811.1, ECO:0000313|Proteomes:UP000033121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106054 {ECO:0000313|EMBL:GAO44811.1,
RC ECO:0000313|Proteomes:UP000033121};
RA Miyazawa S., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K., Ohji S.,
RA Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT "Whole genome shotgun sequence of Flavihumibacter petaseus NBRC 106054.";
RL Submitted (APR-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}.
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:GAO44811.1}.
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DR EMBL; BBWV01000004; GAO44811.1; -; Genomic_DNA.
DR RefSeq; WP_046370818.1; NZ_BBWV01000004.1.
DR AlphaFoldDB; A0A0E9N536; -.
DR STRING; 1220578.FPE01S_04_00540; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000033121; 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:UP000033121}.
FT DOMAIN 19..152
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 164..399
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 286
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 780 AA; 85977 MW; 3FDDD84D5D645FF0 CRC64;
MSKETRKSQA LEYHAKGRPG KIEVVPTKEA KTQRDLSLAY SPGVAEPCKE IALNTENVYQ
YTAKGNLVAV ISNGTAVLGL GDIGPEASKP VMEGKGVLFK IFADIDVFDI EVNEKDPVKF
VEIVKALEPT FGGINLEDIK APECFYIEDQ LKKQLNIPVM HDDQHGTAII SAAALLNALE
LQKKKIDKVR FVVNGAGAAA MACVRLYVEL GAKHENFTLF DKDGVLHKGR TDLGDKMPFA
VKQADATLEK AMKDADVFLG LSVGNVLTAE MVQSMARNPI VFAMANPDPE IAYETAVAAR
KDIIMATGRS DYPNQVNNVL GFPFIFRGAL DVRARQINEE MKLAAVRALA DLAKTPVPDI
VNLAYNEKNI VFGPTYIIPK PLDPRLLSTV APAVAKAAMD SGVATVQIKD WNAYSVELNK
RLGLDNQLMR VIGNLARKDP KRVVFAEADN LKILKAAQIA FEEGIAYPIL LGDEKKIREI
ALRNQIELDG LPIIDPRSDD QEEKRKAYGQ IFFQKRQRKG INKYEAFKIM RDRNYYGCMM
VETGDADAMI SGLTRNYDET IRPAIQVIGT EDGVKKIAGM YLLLTKKGPL FLADTTVNFN
PTAEELAEIT LMVAKEVRNF NLTPRIAMLS YSNFGSSASP EAKLVAEARR IVKERNPSLI
VDGEMQASIA FDKKILKENY PFSELVDQDV NTLIFPNLAA GNVAYNLLKE VGGADAIGPI
LLGIKKPVHV LQLGSSVRSI YNMALVAVID AQIKCNKIPT AEIVGKSKWW KKFRKVSRDM
//
