位置:首页 > 蛋白库 > MDH_BURP1
MDH_BURP1
ID   MDH_BURP1               Reviewed;         327 AA.
AC   Q3JKE9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517};
GN   OrderedLocusNames=BURPS1710b_A0795;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01517};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
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; CP000125; ABA52700.1; -; Genomic_DNA.
DR   RefSeq; WP_004187735.1; NC_007435.1.
DR   PDB; 3D5T; X-ray; 2.51 A; A/B/C/D=1-327.
DR   PDBsum; 3D5T; -.
DR   AlphaFoldDB; Q3JKE9; -.
DR   SMR; Q3JKE9; -.
DR   EnsemblBacteria; ABA52700; ABA52700; BURPS1710b_A0795.
DR   GeneID; 56598079; -.
DR   KEGG; bpm:BURPS1710b_A0795; -.
DR   HOGENOM; CLU_040727_2_0_4; -.
DR   OMA; TKGMERG; -.
DR   OrthoDB; 870724at2; -.
DR   EvolutionaryTrace; Q3JKE9; -.
DR   Proteomes; UP000002700; Chromosome II.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_01517; Malate_dehydrog_2; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..327
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000294380"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         12..18
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         106
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         113
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         130..132
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT   STRAND          6..12
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           16..26
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   TURN            27..31
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   STRAND          37..42
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           48..59
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   STRAND          66..73
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           75..79
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           99..120
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   STRAND          131..133
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           134..143
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           158..172
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           206..210
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           214..218
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           220..225
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           227..235
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           240..256
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           272..274
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   STRAND          280..288
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   STRAND          291..294
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   HELIX           302..319
FT                   /evidence="ECO:0007829|PDB:3D5T"
FT   TURN            320..322
FT                   /evidence="ECO:0007829|PDB:3D5T"
SQ   SEQUENCE   327 AA;  35015 MW;  2E919ABA6D3F67B3 CRC64;
     MAKPAKRVAV TGAAGQIAYS LLFRIANGDL LGKDQPVILQ LLDLPQAQAA VKGVVMELDD
     CAFPLLAGVV ITDDPKVAFK DADVALLVGA RPRSKGMERK DLLSANAEIF TVQGAALNEV
     ASRDVKVLVV GNPANTNAYI AMKSAPDLPK KNFTAMLRLD HNRALSQLAA KSGKPVASIE
     KLAVWGNHSP TMYPDFRFAT AEGESLLKLI NDDVWNRDTF IPTVGKRGAA IIEARGLSSA
     ASAANAAIDH VRDWVLGTNG KWVTMGIPSD GSYGIPEDII YGVPVICENG EYKRVEGLEI
     DAFSREKMDG TLAELLEERD GVAHLLK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024