ID N8WB33_9GAMM Unreviewed; 370 AA.
AC N8WB33;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-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=F966_02762 {ECO:0000313|EMBL:ENV09116.1};
OS Acinetobacter higginsii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=70347 {ECO:0000313|EMBL:ENV09116.1, ECO:0000313|Proteomes:UP000013209};
RN [1] {ECO:0000313|EMBL:ENV09116.1, ECO:0000313|Proteomes:UP000013209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 56.2 {ECO:0000313|EMBL:ENV09116.1,
RC ECO:0000313|Proteomes:UP000013209};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. CIP 56.2.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:ENV09116.1}.
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DR EMBL; APPH01000010; ENV09116.1; -; Genomic_DNA.
DR RefSeq; WP_004806103.1; NZ_KB849440.1.
DR AlphaFoldDB; N8WB33; -.
DR STRING; 1144672.F966_02762; -.
DR PATRIC; fig|1144672.3.peg.2651; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_1_6; -.
DR Proteomes; UP000013209; 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}.
FT DOMAIN 6..355
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 370 AA; 40984 MW; 952392EEE52E3D93 CRC64;
MAKKYKVATI AGDGIGLEVL PEGIKVVKAA ADKYGIQVQM DSFDWASCDY YLEHGKMMPD
NWFEILQQYD AIFFGAVGWP EKVPDHISLW GSLLQFRRRF DQYVNLRPVR LMPGVKCPLA
GKQPGDIDFY VVRENSEGEY SAIGGKAFEG TDREFVLQEA VFTRHGVDRI LKYAFEFADQ
REAKKITAAT KSNGIAVSMP YWDERVDEMA KNYPQIKADK QHVDILAARF VLQPERFDVV
VASNLFGDIL SDLGPACTGT IGLAASANLN PERKFPSLFE PVHGSAPDIY GQQIANPIAA
IWSGAMMLDF LADGDEQVIQ AGQEIMQAIE HVLVHGPKTP DIGGTAKTYE VGDAIASCVT
QQKMDLFAME
//
