GenomeNet

Database: UniProt/TrEMBL
Entry: F5XPH6_MICPN
LinkDB: F5XPH6_MICPN
Original site: F5XPH6_MICPN 
ID   F5XPH6_MICPN            Unreviewed;       329 AA.
AC   F5XPH6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   22-NOV-2017, entry version 47.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS00369716};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517,
GN   ECO:0000313|EMBL:BAK34284.1};
GN   OrderedLocusNames=MLP_12700 {ECO:0000313|EMBL:BAK34284.1};
OS   Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 /
OS   NBRC 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Microlunatus.
OX   NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK34284.1, ECO:0000313|Proteomes:UP000007947};
RN   [1] {ECO:0000313|EMBL:BAK34284.1, ECO:0000313|Proteomes:UP000007947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC   / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA   Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A.,
RA   Sasagawa M., Fukada J., Nakamura S., Katano Y., Hanada S.,
RA   Kamagata Y., Nakamura N., Yamazaki S., Fujita N.;
RT   "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000256|HAMAP-Rule:MF_01517,
CC       ECO:0000256|SAAS:SAAS00755561}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC       {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU004066,
CC       ECO:0000256|SAAS:SAAS00369698}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01517}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP012204; BAK34284.1; -; Genomic_DNA.
DR   RefSeq; WP_013862167.1; NC_015635.1.
DR   ProteinModelPortal; F5XPH6; -.
DR   STRING; 1032480.MLP_12700; -.
DR   EnsemblBacteria; BAK34284; BAK34284; MLP_12700.
DR   KEGG; mph:MLP_12700; -.
DR   eggNOG; ENOG4105D9Z; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000007947; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR001252; Malate_DH_AS.
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.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007947};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369, ECO:0000313|EMBL:BAK34284.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007947};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        5    149       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      156    322       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      11     17       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     129    131       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING      98     98       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     105    105       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     112    112       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     131    131       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
SQ   SEQUENCE   329 AA;  34397 MW;  1FE46B54C465E21B CRC64;
     MSTPVKVAVT GAAGQIGYSL LFRIASGSLL GPDTPVQLRL LEITPALKAL EGVVMELDDC
     AFPLLAGVET GDDPNVVFDG ANIALLVGAR PRTKGMERGD LLEANGAIFK PQGAALNAHA
     ADDIKVLVTG NPANTNALIA KSNAPDIPAE RFNALTRLDH NRALAQLAAK TGSTVNDITK
     MTIWGNHSAT QYPDVFHSEV NGRNAAELID DQDWLESTFI PTVQQRGAAI IAARGASSAA
     SAANATVDHM RDWVLGTPEG DWVSMAVPSD GSYGIAEGII TSFPCTTAGG AYNIVQGLEL
     NEFSRAKIDA SVAELQGERE AVQALGLVE
//
DBGET integrated database retrieval system