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Database: UniProt
Entry: A0A098STM7_9PSED
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ID   A0A098STM7_9PSED        Unreviewed;       562 AA.
AC   A0A098STM7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   25-APR-2018, entry version 22.
DE   RecName: Full=NAD-dependent malic enzyme {ECO:0000256|HAMAP-Rule:MF_01619};
DE            Short=NAD-ME {ECO:0000256|HAMAP-Rule:MF_01619};
DE            EC=1.1.1.38 {ECO:0000256|HAMAP-Rule:MF_01619};
GN   Name=maeA {ECO:0000256|HAMAP-Rule:MF_01619};
GN   ORFNames=LT42_14485 {ECO:0000313|EMBL:KGF63142.1};
OS   Pseudomonas lutea.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=243924 {ECO:0000313|EMBL:KGF63142.1, ECO:0000313|Proteomes:UP000029719};
RN   [1] {ECO:0000313|EMBL:KGF63142.1, ECO:0000313|Proteomes:UP000029719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17257 {ECO:0000313|EMBL:KGF63142.1,
RC   ECO:0000313|Proteomes:UP000029719};
RA   Kwak Y., Shin J.-H.;
RT   "Genome sequence of Pseudomonas lutea strain DSM 17257T.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = pyruvate + CO(2) + NADH.
CC       {ECO:0000256|HAMAP-Rule:MF_01619, ECO:0000256|SAAS:SAAS00632804}.
CC   -!- CATALYTIC ACTIVITY: Oxaloacetate = pyruvate + CO(2).
CC       {ECO:0000256|HAMAP-Rule:MF_01619, ECO:0000256|SAAS:SAAS00632777}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01619, ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01619, ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|HAMAP-Rule:MF_01619, ECO:0000256|PIRSR:PIRSR000106-
CC       3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00632794};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01619,
CC       ECO:0000256|SAAS:SAAS00632781}.
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|HAMAP-Rule:MF_01619, ECO:0000256|RuleBase:RU003427,
CC       ECO:0000256|SAAS:SAAS00632787}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KGF63142.1}.
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DR   EMBL; JRMB01000002; KGF63142.1; -; Genomic_DNA.
DR   RefSeq; WP_037013985.1; NZ_JRMB01000002.1.
DR   EnsemblBacteria; KGF63142; KGF63142; LT42_14485.
DR   GeneID; 36010898; -.
DR   Proteomes; UP000029719; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10380; -; 1.
DR   HAMAP; MF_01619; NAD_malic_enz; 1.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR023667; NAD_malic_enz_proteobac.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000029719};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01619,
KW   ECO:0000256|PIRSR:PIRSR000106-3, ECO:0000256|RuleBase:RU003427,
KW   ECO:0000256|SAAS:SAAS00632801};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01619, ECO:0000256|SAAS:SAAS00632802};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01619,
KW   ECO:0000256|SAAS:SAAS00632803, ECO:0000313|EMBL:KGF63142.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029719}.
FT   DOMAIN       78    258       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      268    528       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   ACT_SITE    101    101       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01619, ECO:0000256|PIRSR:PIRSR000106-
FT                                1}.
FT   ACT_SITE    172    172       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01619, ECO:0000256|PIRSR:PIRSR000106-
FT                                1}.
FT   METAL       243    243       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_01619,
FT                                ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       244    244       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_01619,
FT                                ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       267    267       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_01619,
FT                                ECO:0000256|PIRSR:PIRSR000106-3}.
FT   BINDING     154    154       NAD. {ECO:0000256|HAMAP-Rule:MF_01619}.
FT   BINDING     267    267       NAD. {ECO:0000256|HAMAP-Rule:MF_01619}.
FT   BINDING     415    415       NAD. {ECO:0000256|HAMAP-Rule:MF_01619}.
FT   SITE        267    267       Important for activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01619}.
SQ   SEQUENCE   562 AA;  61933 MW;  1C2BBFE14AD9AAAF CRC64;
     MTKTSRPLYI SYAGPSLLEM PLLNKGSAFT PQERIDFNLV GLLPQNVETI EEQVTRVYSQ
     YQQCASDLDK HIYLRSIQDN NETLFFRLLD SHLDEMLPII YTPTVGQACQ EFSKIYRTHR
     GLFISYPERD RIDDILRSAT KDRIKIIVVT DSERILGLGD QGIGGMGIPI GKLSLYTACG
     GISPAYTLPI VLDVGTNNKE LLDDPMYMGW RHERVTGKEY EDFIALFIEA VQSRWPDVLL
     QFEDFAQTNA MPLLEKYRDE LCCFNDDIQG TASVAVGTLL AACKAKNETL GQQRVVFLGA
     GSAGCGIAEH IIAAMVIEGL SEAEARKRVM MVDRFGLLTD SMDNLLDFQK NLAQKSGDVE
     GWSSGEGSPE LLDVVANGKP TVLIGVSGQR GLFTEQVIRE MHKHCAKPLV MPLSNPTSKV
     EVTPQEVLTW TNGDALVATG SPFAPVTVGD RTFHIAQCNN SYIFPGIGLG VVASKATRIT
     DKMLMAASNA LAECSPMVTG KGDAVLPPLK EIQQVSKKIA LAVALQAQAE GFALETTEEM
     LVEAIERNFW MPNYRSYRRS AV
//
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