ID J9YYT3_9PROT Unreviewed; 763 AA.
AC J9YYT3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=NAD-binding phosphate acetyl/butyryl transferase malic enzyme {ECO:0000313|EMBL:AFS48081.1};
GN ORFNames=HIMB5_00013430 {ECO:0000313|EMBL:AFS48081.1};
OS alpha proteobacterium HIMB5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=859653 {ECO:0000313|EMBL:AFS48081.1, ECO:0000313|Proteomes:UP000006098};
RN [1] {ECO:0000313|EMBL:AFS48081.1, ECO:0000313|Proteomes:UP000006098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB5 {ECO:0000313|EMBL:AFS48081.1,
RC ECO:0000313|Proteomes:UP000006098};
RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA Friedman R., Venter J.C.;
RL Submitted (SEP-2012) 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; CP003809; AFS48081.1; -; Genomic_DNA.
DR AlphaFoldDB; J9YYT3; -.
DR STRING; 859653.HIMB5_00013430; -.
DR KEGG; apm:HIMB5_00013430; -.
DR PATRIC; fig|859653.3.peg.1312; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000006098; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transferase {ECO:0000313|EMBL:AFS48081.1}.
FT DOMAIN 23..156
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 168..405
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 81..88
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 167
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 292
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 763 AA; 83928 MW; BCA8A47ED90372B6 CRC64;
MKKTKADHYT DKEALEFHTK KKPGKIEIVS SKNMTTKRDL ALAYSPGVAV PVKKISENPE
TAYDYTSKGN LVAVISNGSA ILGLGNLGAL ASKPVMEGKA VLFKRFADID SIDLEIDCSD
ANEIIQSIKN FAPSFGGINL EDIAAPDCFI IEQKLKEILD IPVFHDDQHG TAIITTAALI
NALDISRKSI KDIKVVVNGA GASAIACTEL FKRTGVPHEN VIMLDRKGVI YKGRPEKVDQ
WKSRHAIETK KRTLEDAIDG ADVFLGLSAK GALPKAFVKK MAKNPIIFAC ANPDPEITPE
EIEEVRDDAI IATGRSDYPN QVNNLIGFPY IFRGALDVRS KTINEEMKIA AAHAIANLAR
EDVPDEVVAA MGGNRPHYGK EYIIPSTFDP RLISVIPAAV AKAAMETGVA RKEIKNFDTY
KDELKQRLDP TVTIMNGINN LIKNKQKRIV FADGEDENTL KAAIAFKNSK LGIPILVGKE
AKIKEQIQKI GYDDHFDFEI TNSTDNSKRE KYTKYLFKKL QREQGLLEWD CDRLVRNDRV
IWASCMVACG DADGAVTGNT RRFGASLEKV QQVVGARAGE IMFGLNLVVH KGKTIFVADT
SVHEWPTSQQ LSEIAISAAR VVRLFGFDPK VAFVSHSTFG QPVTSRTEQI REAVEILKNK
KVDFEFDGDM QPDVALNEEY KKLYPFSKIV GNANILVMPG QHAASISYKM IKAFGDSKVI
GPLLIGLGLP IEIAPLRCST SEILNLASIA AYSSDIIDYN LEN
//
