ID F4CRQ5_PSEUX Unreviewed; 387 AA.
AC F4CRQ5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Malic protein NAD-binding protein {ECO:0000313|EMBL:AEA27272.1};
GN OrderedLocusNames=Psed_5135 {ECO:0000313|EMBL:AEA27272.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA27272.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA27272.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
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 -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002593; AEA27272.1; -; Genomic_DNA.
DR RefSeq; WP_013677178.1; NC_015312.1.
DR AlphaFoldDB; F4CRQ5; -.
DR STRING; 675635.Psed_5135; -.
DR KEGG; pdx:Psed_5135; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_034446_2_1_11; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000007809; Chromosome.
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 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; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW ECO:0000256|RuleBase:RU003427};
KW Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT DOMAIN 23..156
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 168..385
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 44
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 167
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 387 AA; 39825 MW; 118309905047A127 CRC64;
MTTAPERPLS TPTRDEIFDA HRGGKLATGL TASLRDQRDL AIAYSPGVAE VSRAIAADAA
VARTHTWADR LVAVVSDGTA VLGLGDIGPR AALPVMEGKS ALFKTFAELD SIPLVLDTTD
VDEIVETLVR LRPSFGAVNL EDVAAPRCFE LERRLVEALD CPVMHDDQHG TAIVLLAALR
GACVVTDRDL GSLRVVVSGA GAAGVACARI LLAAGVRDIV LLDSRGVVDA ARGGEKAALA
AITNPRGITG GIAEAMAGAD VFVGLSGALL DESLLAAMSP GGMVFALSNP DPEVHPDVAA
RYASIVATGR SDFPNQINNV LAFPGVFRGA LDAGARRITE AMKLAAADAI HAVARDELAA
DRIVPSPFDP RVATAVATAV AAAAERG
//
