ID A0A0V8JEZ8_9BACI Unreviewed; 361 AA.
AC A0A0V8JEZ8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=D-malate dehydrogenase (decarboxylating) {ECO:0000256|ARBA:ARBA00013126};
DE EC=1.1.1.83 {ECO:0000256|ARBA:ARBA00013126};
GN ORFNames=AS030_08190 {ECO:0000313|EMBL:KSU85464.1};
OS Fictibacillus enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1017270 {ECO:0000313|EMBL:KSU85464.1, ECO:0000313|Proteomes:UP000054099};
RN [1] {ECO:0000313|EMBL:KSU85464.1, ECO:0000313|Proteomes:UP000054099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1003 {ECO:0000313|EMBL:KSU85464.1,
RC ECO:0000313|Proteomes:UP000054099};
RX PubMed=24343101; DOI=10.1007/s10482-013-0097-9;
RA Dastager S.G., Mawlankar R., Srinivasan K., Tang S.K., Lee J.C.,
RA Ramana V.V., Shouche Y.S.;
RT "Fictibacillus enclensis sp. nov., isolated from marine sediment.";
RL Antonie Van Leeuwenhoek 105:461-469(2014).
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:KSU85464.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNQN01000001; KSU85464.1; -; Genomic_DNA.
DR RefSeq; WP_061970366.1; NZ_KQ758617.1.
DR AlphaFoldDB; A0A0V8JEZ8; -.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000054099; 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 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 Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000054099}.
FT DOMAIN 5..349
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 361 AA; 40548 MW; 404B0D2DAEB62B18 CRC64;
MQHFSIAAIP GDGIGPEVMK EGLKTLRKIE ELHGGIRFSI DVFDWNCHYY LKHHRMMPEN
GLDTLRDYDV ILLGAIGTPE VPDHVSVWEL ILPIRRTFQQ YINLRPIKLL KGLESPLRYK
NHSDLDFIVV RENTEGEYSN MGGRLHENTP YEMAVQNNVF TRYGTERVIN YAFQLAEKRK
AKRLTAATKS NGINHSMPFW DEIVKEVSRQ HPSVQTDIYH IDALAAYFIT RPEQLDVVVG
SNLFGDILTD LGAAIVGGLG MAPSGNINPE KAFPSMFEPI HGSAPDIAGK GIANPIAQIW
SIGLMMEHLG FEEMNHLVVS SIEEVLIEGT IRTPDLGGKN KTFELGDAIH KKMQEVSVQH
N
//
