ID A0A1A0PC48_9MYCO Unreviewed; 551 AA.
AC A0A1A0PC48;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:OBB06844.1};
GN ORFNames=A5662_09880 {ECO:0000313|EMBL:OBB06844.1};
OS Mycobacteriaceae bacterium 1482268.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae.
OX NCBI_TaxID=1834080 {ECO:0000313|EMBL:OBB06844.1, ECO:0000313|Proteomes:UP000091934};
RN [1] {ECO:0000313|EMBL:OBB06844.1, ECO:0000313|Proteomes:UP000091934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1482268.1 {ECO:0000313|EMBL:OBB06844.1,
RC ECO:0000313|Proteomes:UP000091934};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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 -!- 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:OBB06844.1}.
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DR EMBL; LZSH01000129; OBB06844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A0PC48; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000091934; 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; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW ECO:0000256|RuleBase:RU003427}.
FT DOMAIN 74..254
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 264..523
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 97
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 239
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 240
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 263
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 551 AA; 60277 MW; FBD63237F6A37E94 CRC64;
MRTPDGELTG QAKLFDALTT KGTAFTHEER LNYGLLGLLP TAEKTLDQQS DHCWHEFCRR
RDDLDKHIYL RALQDRNETL FYRVLRDHIT ETMPIVYTPT VGVACQRFSE IYRRPRGLFV
SYPDRGRLAE VINNRPHRDP DVIVVTDGQR ILGLGDQGIG GMGIPIGKLS LYTLIGGIDP
GRTLPIVLDV GTDNVELLED PQYLGWRHRR ISDDEYYSFI DDFVAAVHEQ LPNVLLQWED
FATAHALPIL ERYRDKLLTF NDDIQGTAAV TLGALHGASK VAGRPLSQQQ VVMLGAGSAG
VGVMDMVKRE MMAQGLSEAD ALKRIWVVDV HGLLTDDRTD LSKGQRPFAQ PADRVAAWGL
SDAAQLADVV HHVDVGILVG LSTAAGAFTE AIVREMAGKV ERPIIFPLSN PTSHAEAHPA
ELDHWTEGRA LIATGSPFAP LQRDGAARPI AQCNNVYIFP AMGLAVTAAQ ATRVTDDMMR
VAAATLGDAS PALSDPVAPL LPSWSDVPDV ALRIAHAVGR QAIADGVAPA RSDDELAARI
AEVRWTPEYR G
//
