ID K9AH51_9MICO Unreviewed; 372 AA.
AC K9AH51;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN ORFNames=C272_10198 {ECO:0000313|EMBL:EKU46614.1};
OS Brevibacterium casei S18.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=1229781 {ECO:0000313|EMBL:EKU46614.1, ECO:0000313|Proteomes:UP000009879};
RN [1] {ECO:0000313|EMBL:EKU46614.1, ECO:0000313|Proteomes:UP000009879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S18 {ECO:0000313|EMBL:EKU46614.1,
RC ECO:0000313|Proteomes:UP000009879};
RA Sharma R., Singh A., Jangir P.K.;
RT "Genome Sequence of Brevibacterium casei S18.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.85;
CC Evidence={ECO:0000256|ARBA:ARBA00000624};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC Xref=Rhea:RHEA:18365, ChEBI:CHEBI:15361, ChEBI:CHEBI:15588,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.83;
CC Evidence={ECO:0000256|ARBA:ARBA00001361};
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};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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:EKU46614.1}.
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DR EMBL; AMSP01000008; EKU46614.1; -; Genomic_DNA.
DR RefSeq; WP_009378646.1; NZ_AMSP01000008.1.
DR AlphaFoldDB; K9AH51; -.
DR PATRIC; fig|1229781.4.peg.2050; -.
DR eggNOG; COG0473; Bacteria.
DR OrthoDB; 5289857at2; -.
DR Proteomes; UP000009879; Unassembled WGS sequence.
DR GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR011829; TTC_DH.
DR NCBIfam; TIGR02089; TTC; 1.
DR PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000009879}.
FT DOMAIN 8..354
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 372 AA; 39677 MW; CEB7F98E894C06DD CRC64;
MTDTQTFSIA SIPGDGIGGE VVAAGLRVLD TVAKLSDGDI AFDVTEYPWS SAYYLEHGTY
IPEGGLEDLR KHDAIYFGAV GSADVPDHTS LWGLRLAITQ PFDQWANIRP VTFLPGVESP
LRKADDTDLD WIVVRENSEG EYAGMGGRNL SGRGPGNEVA LQTSLHTEKG TERIIRFAFD
LARTRAVKKV SSVTKSNAQQ YGMVLWDEVF ARVAADYPDV ETESVLVDAM SAKFVLHPEQ
LSVVVASNLH ADILSDLGSA LAGSLGLAAS ANLNPEKRFP SMFEPVHGSA PDIAGLGVSN
PIGAISSAAL MLDDFGLHQE ADEVRRAIEN VTAAGILPRD LGGESNTIEM TEAIVAQLEA
LHAEAAVPEP SH
//
