ID I4BMV2_MYCCN Unreviewed; 409 AA.
AC I4BMV2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:AFM18609.1};
GN OrderedLocusNames=Mycch_3884 {ECO:0000313|EMBL:AFM18609.1};
OS Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM18609.1, ECO:0000313|Proteomes:UP000006057};
RN [1] {ECO:0000313|EMBL:AFM18609.1, ECO:0000313|Proteomes:UP000006057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB4 {ECO:0000313|EMBL:AFM18609.1,
RC ECO:0000313|Proteomes:UP000006057};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium chubuense NBB4.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR EMBL; CP003053; AFM18609.1; -; Genomic_DNA.
DR AlphaFoldDB; I4BMV2; -.
DR STRING; 710421.Mycch_3884; -.
DR KEGG; mcb:Mycch_3884; -.
DR PATRIC; fig|710421.3.peg.3880; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_034446_2_1_11; -.
DR Proteomes; UP000006057; 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 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; 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 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 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006057}.
FT DOMAIN 40..173
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 185..405
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 409 AA; 42279 MW; CC7DEACD8BBF60C1 CRC64;
MKYPDAVAES VVVPSRDPSS AGRTPQVVVE DTEIFEAHEG GKLSIGLNSP LDTQRALSIA
YTPGVAKVSR AIATDRTLAA KYTWAHRLVA VVSDGSAVLG LGDIGASASL PVMEGKSALF
KTFGGLDSIP IVLDTKDPDE IVETLIRLRP TFGAVNLEDI SAPRCFEIER RVIEALDCPV
MHDDQHGTAI VVLGALLGAC KVLDRDMHTL RVVISGAGAA GVACANILLA KGISDITVLD
SKGIVHTGRS DLNSFKAELA ERTNPSGRTG GVAEAVDGAD MFLGLSAGVV PEEIIATMAP
GGIVFALSNP DPEIHPDAAR KYAAVVATGR SDFPNQINNV LAFPGVFRGA LDAGARRITE
KMKVAAAEAI FSVVGDDLAA DHIVPSALDP RVGPAVAAAV AAASEDSVG
//
