ID A1K3N3_AZOSB Unreviewed; 758 AA.
AC A1K3N3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Probable malate dehydrogenase (Oxaloacetate-decarboxylating) (NADP+) {ECO:0000313|EMBL:CAL93438.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:CAL93438.1};
GN Name=maeB1 {ECO:0000313|EMBL:CAL93438.1};
GN OrderedLocusNames=azo0821 {ECO:0000313|EMBL:CAL93438.1};
OS Azoarcus sp. (strain BH72).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL93438.1, ECO:0000313|Proteomes:UP000002588};
RN [1] {ECO:0000313|EMBL:CAL93438.1, ECO:0000313|Proteomes:UP000002588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72 {ECO:0000313|EMBL:CAL93438.1,
RC ECO:0000313|Proteomes:UP000002588};
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL93438.1; -; Genomic_DNA.
DR RefSeq; WP_011764555.1; NC_008702.1.
DR AlphaFoldDB; A1K3N3; -.
DR STRING; 62928.azo0821; -.
DR KEGG; azo:azo0821; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_4; -.
DR Proteomes; UP000002588; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
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,
KW ECO:0000313|EMBL:CAL93438.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002588}.
FT DOMAIN 18..151
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 163..400
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 76..83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 136
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 287
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 758 AA; 82219 MW; 0D7D8970032FF7E9 CRC64;
MDELIRAAAL DYHRYPRPGK IAVAPTKVLS NQRDLSLAYS PGVAAACDAI VEDPAEAANL
TSRSNLIGVI TNGTAVLGLG NIGALAAKPV MEGKGVLFKK FAGIDVFDLE IAEPDPDKLI
DMIAALEPTF GGINLEDIKA PECFYIESKL RERMKIPVFH DDQHGTAIVV GAAILNGLQM
QGKDLKQVKL VTSGAGAAAL ACLGLLVKLG VPVENIWVTD LEGVVYEGRT ALMDPIKARY
AKKTEARKLA EVIEGADVFL GLSAGGVLKG EMVAKMAAKP LILALANPTP EILPEEVKAV
RDDAIIATGR SDYPNQVNNV LCFPFIFRGA LDVGATTITD EMQLAAVRAI AELARAEQSD
IVAAAYGEKV SGFGTEYIIP RPFDPRLIVK IAPAVAEAAM SSGVATRPIT DWDAYRGHLN
NFVWHSGLLM KPVFAAAKKA PKRIIFSEGE SEKVLRAVQT VIDEGMARPI LIGRPDVIAN
NITRFGLRME AERDFELVNP ESDPRFKELW THYHALTERK GVSVEYAKKE VRRRTTLIGS
LLLKFGYGDG LICGTYGMHR LHLDFVETVL GRREGVNHCY TLNVLSLPER TLFLADTYVN
YDPTPEQVVE MTRLAAEEMQ RFGVEPRVAL LSHSSFGSAD SPTAEKMRTA LRLLHERHSE
LQVEGEMHGD SALDAKLRTQ IFPNARMRED ANLLIFPTLD AANIAFNLLK SAAGEGMTVG
PILLGAAKPV HILTPSATVR RIINMTALTV VEAGQQGA
//
