ID I0I2J2_CALAS Unreviewed; 746 AA.
AC I0I2J2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:BAL99479.1};
GN Name=maeB {ECO:0000313|EMBL:BAL99479.1};
GN OrderedLocusNames=CLDAP_14400 {ECO:0000313|EMBL:BAL99479.1};
OS Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS STL-6-O1).
OC Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC Caldilinea.
OX NCBI_TaxID=926550 {ECO:0000313|EMBL:BAL99479.1, ECO:0000313|Proteomes:UP000007880};
RN [1] {ECO:0000313|EMBL:BAL99479.1, ECO:0000313|Proteomes:UP000007880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC {ECO:0000313|Proteomes:UP000007880};
RA Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Hanada S., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT 102666).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; AP012337; BAL99479.1; -; Genomic_DNA.
DR RefSeq; WP_014432718.1; NC_017079.1.
DR AlphaFoldDB; I0I2J2; -.
DR STRING; 926550.CLDAP_14400; -.
DR KEGG; cap:CLDAP_14400; -.
DR PATRIC; fig|926550.5.peg.1519; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_0; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000007880; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Metal-binding {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:UP000007880}.
FT DOMAIN 17..150
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 162..399
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 75..82
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 135
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 136
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 161
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 746 AA; 82276 MW; 61C6F5ED94EF0307 CRC64;
MGNLKQDSLD YHAQGRPGKL KIVATKPMET QRDLSLAYSP GVAYPVLAIA ENPEVAFDYT
AKGNLVAVIS NGTAILGLGD RGPLAAKPVM EGKAVLFKRF ADVDVFDIEV NSKDPEEIVR
FGEMIAPTFG GINLEDIKAP ECFYIETELQ RRVDIPVFHD DQHGTAIISG AGLLNALELV
GKRIDQIKVV MNGAGAASIA TAELYVALGV RKENIILCDT KGVIYKGREV GMNEYKARYA
SDTTARTLEE AMVDADVFIG LSVANCVTRE MVRSMARDPI LFAMANPDPE ITYEEVQAAR
SDVIFGTGRS DYPNQVNNVL GFPFIFRGAL DVRARKVNME MKLAATRALA ALAKEDVPDS
VIRAYGLSEL RFGREYIIPK PLDPRVMLWV APAVAKAAME TGVARRHLDL DEYINMLKAR
QGKGAQTMHM LEQKARKAPK RIVFGEGREP RVIRAAHEVE VNGVAKPILL GHVEEVRRQI
RELGLNWEPE IIDPIDSPRH GEYAEHFYHK RQRKGVTLSR ARELMRQKMY YGPMMVEMGD
ADAFIAGLAY NYPEVLRPAL QCVGAQDGRW VSGVYMMLVQ DRMFFFTDAT VIIDPTAEQL
AAIALNAADL AERFGVRPRI AMLSFSNFGS TPHPSQQKVQ QATELVRRQR PDLEIDGEMQ
ADVAVSPELM KRHYPFSRVS DANVLVFPDL ASANTSYKLL SQLGGAEAIG PILVGMAKPI
HVLATGAEVR DIVNVATIAV IDAQSR
//
