ID B0CGG8_BRUSI Unreviewed; 774 AA.
AC B0CGG8;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP(+)), Phosphate acetyltransferase {ECO:0000313|EMBL:ABY38119.1};
GN OrderedLocusNames=BSUIS_A1060 {ECO:0000313|EMBL:ABY38119.1};
OS Brucella suis (strain ATCC 23445 / NCTC 10510).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=470137 {ECO:0000313|EMBL:ABY38119.1, ECO:0000313|Proteomes:UP000008545};
RN [1] {ECO:0000313|EMBL:ABY38119.1, ECO:0000313|Proteomes:UP000008545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23445 / NCTC 10510 {ECO:0000313|Proteomes:UP000008545};
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL Submitted (DEC-2007) 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; CP000911; ABY38119.1; -; Genomic_DNA.
DR RefSeq; WP_002964135.1; NC_010169.1.
DR AlphaFoldDB; B0CGG8; -.
DR GeneID; 3787692; -.
DR KEGG; bmt:BSUIS_A1060; -.
DR PATRIC; fig|359391.4.peg.1080; -.
DR HOGENOM; CLU_012366_0_0_5; -.
DR Proteomes; UP000008545; Chromosome I.
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:ABY38119.1}.
FT DOMAIN 27..160
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 172..409
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 85..92
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 171
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 296
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 774 AA; 83787 MW; 916C1883FE12CB0A CRC64;
MTKKPSSPST RSDFDEAALF FHRYPKPGKL EIQATKPLGN QRDLALAYSP GVAAPCLAIH
DDPATAAEYT ARGNLVAVVS NGTAVLGLGN IGALASKPVM EGKAVLFKKF ADIDVFDIEI
DAHEINRIVD VVSALEPTFG GINLEDIKAP ECFEVEEQLR ERMNIPVFHD DQHGTAIIVA
SAVLNGLELA GKKIEEAKIV TSGAGAAALA CLNLLVNLGA KRENIWVCDI EGVVYDGRNT
LMDRWKEVYA QKTDARTLAD VIGGADVFLG LSAAGVLKPE LLKQMAEKPL IMALANPKPE
IMPEEARAAR ADAMICTGRS DFPNQVNNVL CFPYIFRGAL DVGATVINEE MKLAAVRAIA
SLAREEPSDV AARAYSGDTP TFGPDYIIPS PFDQRLILRI APAVAKAAME TGVATRPIED
MEAYLDRLNR FVFRSGLIMK PVFAAARTQG APMRVIYADG EDERVLRAAQ VVIEERIAAP
ILVGRPQVVE TRLRRYGLKI RPGTDFELIN PEDDPRYRDY VDLYLSYTGR QGVTPEAART
IVRTNSTAIA ALAVMRDEAD AMICGLEGRF ERHLRVVRQI IGKVPGIRDY SALSLLISQR
GALFLTDTYV NAEPDANEIA EMAVLAAREI SRFGIEPKAA LVSHSNFGSK ESASAEKMRQ
AAAILAEKAP DLESDGEMHG DAALSQTLRD RVFPSSRLKG EANLLVFPNL DAANITLNVV
KAVTDALHVG PILLGATRPA HILTPSVTSR GVVNMTALAV VEALQKNASN RRQK
//
