ID A0A260BRU7_9NOCA Unreviewed; 554 AA.
AC A0A260BRU7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:OZD06527.1};
GN ORFNames=CH275_09925 {ECO:0000313|EMBL:OZD06527.1};
OS Rhodococcus sp. 06-235-1A.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2022508 {ECO:0000313|EMBL:OZD06527.1, ECO:0000313|Proteomes:UP000215839};
RN [1] {ECO:0000313|EMBL:OZD06527.1, ECO:0000313|Proteomes:UP000215839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=06-235-1A {ECO:0000313|EMBL:OZD06527.1,
RC ECO:0000313|Proteomes:UP000215839};
RA Savory E.A., Fuller S.L., Weisberg A.J., Thomas W.J., Gordon M.I.,
RA Stevens D.M., Creason A.L., Belcher M.S., Wiseman M., Putnam M.L.,
RA Grunwald N.J., Chang J.H.;
RT "Evolutionary transitions between beneficial and phytopathogenic
RT Rhodococcus challenge disease management.";
RL Submitted (JUL-2017) 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:OZD06527.1}.
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DR EMBL; NOYI01000011; OZD06527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A260BRU7; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000215839; Unassembled WGS sequence.
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:0008152; P:metabolic process; IEA:UniProt.
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; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 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; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3}.
FT DOMAIN 68..254
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 260..516
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 91
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 236
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 259
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 554 AA; 59132 MW; 26EE02E29E8AA661 CRC64;
MDNGQHVLRD AHLNRGTAFT SEQRRALGLT GRLPASVETV EAQAARSYQQ LGSQPDDLAK
YVYLNALHDR NETLYFRLLT DHLAELLPVV YDPTIGDAIE QWSHEYRRSR ALYLSVDQIG
DVRASFETLG LGPDDVDLIV CSDAEEILGI GDWGVNGTDI AVGKLAIYTA AAGIDPHRVI
AVNLDVGTDN QELLDDPAYL GNRHERVRGE KYDELIDTYL DVASDLFPHA LLHFEDFGPS
NARRILIEHG ERHRIFNDDM QGTGAIVMAA VMSGMKVTGG RFADQRLVVF GAGTAGTGMA
DQISAAMVAD GLTLEQARAR VWLIDKDGLV TDDMDHLPDY QQPYARPAAE VTDAGGTVDL
LSVVESVHPT ILIGTSTVAG AFTEDVVRAL CAGVERPVLL PLSNPTSRIE VIPRDAIAWS
DGNALVATGI PADPVERDGV TYHIGQGNNA LLYPGLGLGT IVAGASRVTD GMLLAAANAV
AEQVDVGARG ASLLPPVEDL RASSAIVAAA VARAAASDGV ATKVHGDLDA AVREAMWTPQ
YPPLDLASEM EAGR
//
