ID A0A157ZC64_9BURK Unreviewed; 764 AA.
AC A0A157ZC64;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:SAK43111.1};
GN ORFNames=AWB75_00502 {ECO:0000313|EMBL:SAK43111.1};
OS Caballeronia catudaia.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1777136 {ECO:0000313|EMBL:SAK43111.1, ECO:0000313|Proteomes:UP000054870};
RN [1] {ECO:0000313|EMBL:SAK43111.1, ECO:0000313|Proteomes:UP000054870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29318 {ECO:0000313|EMBL:SAK43111.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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; FCOF02000002; SAK43111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A157ZC64; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000054870; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 22..155
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 167..404
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 80..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 166
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 291
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 764 AA; 82915 MW; D1D4C0D144CC359E CRC64;
MTTDANTKLR EAALDYHEFP VPGKIAIAPT KQMINQRDLA LAYSPGVAFA CEAIVEDPLN
AARFTARSNL VGVVSNGTAV LGLGNIGPLA SKPVMEGKAV LFKKFAGIDV FDIELNETDP
HKLVDVIAAL EPTFGGINLE DIKAPDCFIV ERECRKRMKI PVFHDDQHGT AIVVAAAITN
GLKVVGKNIG EVKLVASGAG AAALACLNLL VDLGMKRENI YVTDLAGVVY KGRTELMDPD
KEQFARETSA RTLAEVMEGA DVFLGLSAGG VLKQDMVKQM AAKPLILALA NPTPEILPEL
ALEVRPDAVL ATGRTDYPNQ VNNVLCFPFI FRGALDVGAT VITKEMEIAA VNAIAELARQ
EQSDIVATAY GIQDLSFGPE YLIPKPFDPR LIVKIAPAVA RAAMESGVAT RPIEDMDAYE
QHLQQFVYHS GTTMKPVFQL ARSVEPDKKR IVFAEGEEER VLRAVQIAVD EKIAKPILIG
RPAVIEQRIQ KFGLRLTPGA DFTVVDTDHD ERYRDFWQTY YKMMARKGIS EQMAKLEMRR
RTTLIGAMLV RKGEADGMIC GTVSTTHRHL HFIDQVIGKK EGAKVYAAMN ALVLPGRQIF
IVDTHVNVDP TPEQLAEITI MAAEEVKRFG ILPKIALLSH SNFGTSNAPT AQKMRDVLAI
LRERAPDLDV DGEMHGDVAL DARLRKDVLP ESTLEGDANL LILPNIDAAN ISYNLLKTAA
GNNIAIGPIL LGAAQPVHVL TSSATVRRIV NMTALLVADA SAAR
//
