ID R4Z6S9_9ACTN Unreviewed; 337 AA.
AC R4Z6S9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Putative tartrate dehydrogenase {ECO:0000313|EMBL:CCM65611.1};
GN Name=yeaU {ECO:0000313|EMBL:CCM65611.1};
GN ORFNames=BN381_80141 {ECO:0000313|EMBL:CCM65611.1};
OS Candidatus Microthrix parvicella RN1.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Microthrixaceae; Candidatus Microthrix.
OX NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM65611.1, ECO:0000313|Proteomes:UP000018291};
RN [1] {ECO:0000313|EMBL:CCM65611.1, ECO:0000313|Proteomes:UP000018291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN1 {ECO:0000313|EMBL:CCM65611.1,
RC ECO:0000313|Proteomes:UP000018291};
RX PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT based on genomic and metagenomic analyses.";
RL ISME J. 7:1161-1172(2013).
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 -!- 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 -!- 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:CCM65611.1}.
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DR EMBL; CANL01000078; CCM65611.1; -; Genomic_DNA.
DR RefSeq; WP_012230491.1; NZ_HG422565.1.
DR AlphaFoldDB; R4Z6S9; -.
DR STRING; 1229780.BN381_80141; -.
DR GeneID; 78312341; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_1_11; -.
DR Proteomes; UP000018291; Unassembled WGS sequence.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
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.
PE 4: Predicted;
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:UP000018291}.
FT DOMAIN 10..331
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 337 AA; 36174 MW; 5251F1ABCA5E801B CRC64;
MTSTKNPPHH VGVIGGDGIG PEVTAQALRV LEAAGLQMEL THYDLGAARF LRDGTVLPDE
TMAEWRGLDA LLLGAVGDPA PGQAAPAGLV ERGILLRMRF ELDMYVNYRP FRLPPTVNFE
VIRENTEGTY AGEGGFLRKN TPNEIATQGS VNTRHGVERC IRYSFEQAAN SERHHLTLVH
KKNVLTFAGD LWQRAFDEVA VEYPQVETAY QHVDAACIHF VERPEIYDVV VTDNLFGDIL
TDLAGAVAGG VAYAASANLN PDRTGPSMFE PVHGTAPDIA GKNIANPIAA VISAGLMAGF
LGETEVAEAI EIATADPRRY VGSTSEIGDA LVAAVTR
//