ID A0A090Y9K6_PAEMA Unreviewed; 467 AA.
AC A0A090Y9K6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ACT domain protein {ECO:0000313|EMBL:KFM94502.1};
GN ORFNames=DJ90_1478 {ECO:0000313|EMBL:KFM94502.1};
OS Paenibacillus macerans (Bacillus macerans).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44252 {ECO:0000313|EMBL:KFM94502.1, ECO:0000313|Proteomes:UP000029278};
RN [1] {ECO:0000313|EMBL:KFM94502.1, ECO:0000313|Proteomes:UP000029278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8244 {ECO:0000313|EMBL:KFM94502.1,
RC ECO:0000313|Proteomes:UP000029278};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFM94502.1}.
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DR EMBL; JMQA01000047; KFM94502.1; -; Genomic_DNA.
DR RefSeq; WP_036618915.1; NZ_UGSI01000002.1.
DR AlphaFoldDB; A0A090Y9K6; -.
DR STRING; 44252.DJ90_1478; -.
DR GeneID; 77010841; -.
DR PATRIC; fig|44252.3.peg.5754; -.
DR HOGENOM; CLU_034446_2_1_9; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000029278; Unassembled WGS sequence.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) 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 CDD; cd05311; NAD_bind_2_malic_enz; 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; IPR002912; ACT_dom.
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; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000029278}.
FT DOMAIN 7..80
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 205
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 206
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 231
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 467 AA; 49631 MW; F9C251D235CE1ABA CRC64;
MATTLIIIRL ELDHEHASFG DVAAAVSQAG GDITSIDVIS SAKGSSIRDI TVDTGDRDEA
AIVGALRRLP GVRLINVSDR TFLMHLGGKI SIKPTLPIRN RDDLSQVYTP GVAKVCKAIH
ESPAKAFSLT IKRNTVAVIT DGTAVLGLGG IGPYAAAPVM EGKAMLFKQL AGVDAFPLCL
DTSDTEEIIR TVKAVAPIFG GINLEDISSP RCFEIERRLA EELDIPVFHD DQHGTAVVVT
AGLINALKVV GKRMSEVRVV VSGVGAAGVS ICKMLLAAGV TRLVPVDRAG AIVFGGKYEH
PMWQWLAEQP QVEARAGALK DVLPGADVFI GVSSGGLLAG ADIRAMNERP IVFALANPEP
EIKPEEALKH AAVVATGRSD YPNQINNVLV FPGLFRGALD CRARRINEAM KLAAAEAIAS
SVTDEERNEQ YIIPSIFNDQ VVPLVRKAIV IAAISTGVAR RIPPDFR
//
