GenomeNet

Database: UniProt
Entry: D4YP25_9MICO
LinkDB: D4YP25_9MICO
Original site: D4YP25_9MICO 
ID   D4YP25_9MICO            Unreviewed;       330 AA.
AC   D4YP25;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:EFG46982.1};
DE            EC=1.1.1.37 {ECO:0000313|EMBL:EFG46982.1};
GN   Name=mdh {ECO:0000313|EMBL:EFG46982.1};
GN   ORFNames=HMPREF0183_1685 {ECO:0000313|EMBL:EFG46982.1};
OS   Brevibacterium mcbrellneri ATCC 49030.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=585530 {ECO:0000313|EMBL:EFG46982.1, ECO:0000313|Proteomes:UP000005714};
RN   [1] {ECO:0000313|EMBL:EFG46982.1, ECO:0000313|Proteomes:UP000005714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49030 {ECO:0000313|EMBL:EFG46982.1,
RC   ECO:0000313|Proteomes:UP000005714};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613}.
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:EFG46982.1}.
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; ADNU01000047; EFG46982.1; -; Genomic_DNA.
DR   RefSeq; WP_005884919.1; NZ_ADNU01000047.1.
DR   AlphaFoldDB; D4YP25; -.
DR   STRING; 585530.HMPREF0183_1685; -.
DR   eggNOG; COG0039; Bacteria.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000005714; Unassembled WGS sequence.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW   ECO:0000313|EMBL:EFG46982.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005714}.
FT   DOMAIN          4..141
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          154..321
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         8..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         101
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   330 AA;  34802 MW;  B6097F314681A319 CRC64;
     MKIVAVSGAA GNIGYNVLGR LADGYVYGDE PIELRLLEVP QAVQALDGVI MELVDHASPR
     IANIVATDDP EVAFDGAHAA LLIGSAPRKD GMTRGDLLEV NAGIFSTQGR VLGQVAHPDC
     KVVVTGNPAN TNALVAAHHA EKEGFNPANI TALTRLDHNR LIGQVAQRAR VSAGDIAQVA
     VWGNHSNTQF PDLTFATVGG TPALDVIDRD TWLDTIVPTV ATRGGAVIQA RGGSSVVSAA
     SATLDHLRDW EQGTDGRWVS MAVPTQALPE EARYGVPAGV VYSYPVTIEN GTYTVVPQLE
     LDDLQRERIT ASANELLDER STAAGKGHLD
//
DBGET integrated database retrieval system