ID A0A261QIV4_9BACI Unreviewed; 418 AA.
AC A0A261QIV4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:OZI12282.1};
GN ORFNames=CEW92_07355 {ECO:0000313|EMBL:OZI12282.1};
OS Bacillaceae bacterium SAS-127.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=2015203 {ECO:0000313|EMBL:OZI12282.1, ECO:0000313|Proteomes:UP000217062};
RN [1] {ECO:0000313|EMBL:OZI12282.1, ECO:0000313|Proteomes:UP000217062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAS-127 {ECO:0000313|EMBL:OZI12282.1,
RC ECO:0000313|Proteomes:UP000217062};
RA Verma A., Pal Y., Krishnamurthi S.;
RT "Indiibacillus sp. (SAS-127) genome sequencing.";
RL Submitted (JUN-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}.
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:OZI12282.1}.
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DR EMBL; NKXN01000030; OZI12282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261QIV4; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000217062; 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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000217062}.
FT DOMAIN 16..149
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 161..385
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 37
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 134
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 135
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 160
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 418 AA; 44784 MW; 73E8F179D9F8143E CRC64;
MHNLREDALE IHRHHQGKLE TSAKLNVKNV KDLSLVYSPG VAEPCLEIHA HPEKIYEYTM
KANTVAVVSD GTAVLGLGDI GADASLPVME GKAILFKNFA GVDAFPICID TKDPEEVIKT
VKLLQSSFGG INLEDIKAPN CFLIEERLKK ETDIPIFHDD QHGTAIVTLA GLINSLKLVH
KTFNDIKVVI NGAGAAGIAI AKLLYSFGVK EIIMCDSKGA IYAGRPHGMN SVKEEIATFT
NPNRIEGTLE KAIINSDVFI GVSAAGALTS EMVRTMAQDP IVFAMANPNP EIDPIEAKAA
GVKIIGTGRS DFPNQVNNVL AFPGIFRGAL DTRATDINEE MKIAAAHAIA SLIADHELAD
DYIIPSAFDA RVAPEVAAAV AAAAIHSGVA RQHINVDSLR HKTYQLSAIQ VKPAEIIL
//
