ID A0A1N7QHA8_9FLAO Unreviewed; 764 AA.
AC A0A1N7QHA8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Allosteric NADP-dependent malic enzyme {ECO:0000313|EMBL:SIT22154.1};
GN ORFNames=SAMN05421785_111152 {ECO:0000313|EMBL:SIT22154.1};
OS Chryseobacterium gambrini.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=373672 {ECO:0000313|EMBL:SIT22154.1, ECO:0000313|Proteomes:UP000185781};
RN [1] {ECO:0000313|EMBL:SIT22154.1, ECO:0000313|Proteomes:UP000185781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18014 {ECO:0000313|EMBL:SIT22154.1,
RC ECO:0000313|Proteomes:UP000185781};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTOV01000011; SIT22154.1; -; Genomic_DNA.
DR RefSeq; WP_076395247.1; NZ_FTOV01000011.1.
DR AlphaFoldDB; A0A1N7QHA8; -.
DR STRING; 373672.SAMN05421785_111152; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000185781; 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 25..158
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 170..406
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 83..90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 144
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 293
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 764 AA; 85002 MW; 0A837FD2C7930B97 CRC64;
MSSKTHRDEK NFNQAALDYH KAEPKGKIEV IPSKPHSSQR DLSLAYSPGV AVPCMEIHDK
PETVYDYTGK GNLVAVISNG TAVLGLGDIG AEASKPVMEG KGLLFKIFAD INVFDIEINE
KDPDKFIEIV KGIAPTFGGI NLEDIKAPEA FYIEQRLKEE LDIPLMHDDQ HGTAIISAAA
LINSLQIANK KIEEVKMVVN GAGAAAIACT NLYISLGLKR ENVLMCDSKG VINHKRENLT
PEKIDFVAQT DIETLEDAVK GSDVFVGLSK GNVMTPEMLL SMNENPIVFA LANPDPEIAY
NVALETRKDV IMATGRSDYP NQVNNVLGFP YIFRGALDVQ AKGINEAMKL AAVHAIADLA
KEPVPEAVIL AYNIQNLQFG REYFIPKPFD NRLITKVSSA VAKAAVESGI ARKTITDFEE
YENSLLDRMG RDEKLVRMMQ NRAKANPKRI TLGNAEEYNV LKAAQILYEE GIAYPSLLGN
KKYIKEQMEH FGINLDIPII DPSDDDQKEN RKKYRETLWK LRQRKGMNEY KAKRFVRQRD
YFGPLMLKHG DTDGLIVGFS KNYTSVLRPV LEVIEKDKGV DKVAAMMMIL SEKKPIFFAD
TSINQNPTAE DLVNIAKMAE FTVKSFAIEP RIAMLGFENF AAISETSKKV AKAVSILHEK
YPKMIVDGEI QPDFAMNSDH LSDYPFSKLG TTPANTFIFP NLESANLSYK IIRGMKVAQV
IGPILMGLKQ PVHVLQMRSS VDEIVNLATI AVLDAQRREK KDKK
//
