ID A0A252B9I0_9PROT Unreviewed; 542 AA.
AC A0A252B9I0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:OUJ00870.1};
GN ORFNames=HK20_05535 {ECO:0000313|EMBL:OUJ00870.1};
OS Acetobacter sp. DsW_54.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=1670660 {ECO:0000313|EMBL:OUJ00870.1, ECO:0000313|Proteomes:UP000194822};
RN [1] {ECO:0000313|EMBL:OUJ00870.1, ECO:0000313|Proteomes:UP000194822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DsW_54 {ECO:0000313|EMBL:OUJ00870.1};
RA Ju J., Zhang J.;
RL Submitted (JUN-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 -!- 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:OUJ00870.1}.
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DR EMBL; JOPD01000001; OUJ00870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A252B9I0; -.
DR Proteomes; UP000194822; 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 CDD; cd05312; NAD_bind_1_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; 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:SF90; MALIC ENZYME-RELATED; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000194822}.
FT DOMAIN 73..253
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 263..514
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 96
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 238
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 239
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 262
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 445
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 542 AA; 59927 MW; B445AAFC4B05C042 CRC64;
MPSALTLRGT ALLNNALLNK GTAFTEAERR EYGLEGLLPT QVETLDRQVE RIHRHLEAKP
SNLERYIYLS GLRDQNQTLF YRVLMSNPAQ FVPIVYAPTL AAVCQQFSHI YRRPRGMYIS
LDMRGRIRDV LRNWPTDNVR FLCVTTGGRI LGLGDIGVNG MGIPIGKLDL YTACGAVPPE
VLLPVQLDIG TTNSALRADP LYLGLRREPP PLEELDGFVE EFVSAVKEVF PNCCLHFEDW
KGTDALHYLD KYRNTALCYN DDIQGTAAVT LAGLITALKI KNETLAQQRF LFLGAGSSGL
GTADMLISAL KQEGISEQEA IERITLMDVN GLLETSRTDL SPQQKRYAKA MPPSRDLLAT
IKAIKPTVLI GVSTSGGAFT QEVVETMSAL NERPIIFPLS LPQKNAECTA EQAYEWSQGQ
ALFAAGLQFP EVEMNGRTFY PGQANNFYIF PALGLAVYAT CPKHITDDMV IETARALADQ
VDPASRERGR LFPPQSDILE VSVTSAARIA EFIFDQGAAT VERPKDIRAW IESLTYSPRY
AG
//