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Database: UniProt
Entry: A0A368NS08_9GAMM
LinkDB: A0A368NS08_9GAMM
Original site: A0A368NS08_9GAMM 
ID   A0A368NS08_9GAMM        Unreviewed;       562 AA.
AC   A0A368NS08;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=DU002_02070 {ECO:0000313|EMBL:RCU52956.1};
OS   Corallincola holothuriorum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Corallincola.
OX   NCBI_TaxID=2282215 {ECO:0000313|EMBL:RCU52956.1, ECO:0000313|Proteomes:UP000252558};
RN   [1] {ECO:0000313|EMBL:RCU52956.1, ECO:0000313|Proteomes:UP000252558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 {ECO:0000313|EMBL:RCU52956.1,
RC   ECO:0000313|Proteomes:UP000252558};
RA   Xia H.;
RT   "Corallincola holothuriorum sp. nov., a new facultative anaerobe isolated
RT   from sea cucumber Apostichopus japonicus.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = CO2 + NADH + pyruvate;
CC         Xref=Rhea:RHEA:12653, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.38;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01619};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:16526; EC=1.1.1.38; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01619};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01619,
CC         ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01619,
CC         ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|HAMAP-Rule:MF_01619, ECO:0000256|PIRSR:PIRSR000106-3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01619}.
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|HAMAP-Rule:MF_01619,
CC       ECO:0000256|RuleBase:RU003427}.
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:RCU52956.1}.
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DR   EMBL; QPID01000001; RCU52956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368NS08; -.
DR   OrthoDB; 3314528at2; -.
DR   Proteomes; UP000252558; 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   CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR   Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_01619; NAD_malic_enz; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
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   PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR   PANTHER; PTHR23406:SF34; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01619};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01619};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01619}; Reference proteome {ECO:0000313|Proteomes:UP000252558}.
FT   DOMAIN          78..258
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          268..528
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT                   ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT                   ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         154
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         243
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT                   ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         244
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT                   ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         267
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT   BINDING         267
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01619,
FT                   ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         415
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
FT   BINDING         415
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         459
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   SITE            267
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01619"
SQ   SEQUENCE   562 AA;  61818 MW;  266E14934FD070BA CRC64;
     MMPDKRPVYI PYAGPILLET ALLNKGSGFS ELERREFNLE GLVPSAIESI EEQGERAYLQ
     YKAFESDIYK HIYLRNIQDT NETLFYKLVA DHISEMMPII YTPTVGHACE QFSRNYRRSR
     GLFVSYPDRE RIEDILNNSI RHNVKVIVIT DGERILGLGD QGIGGMGIPI GKLSLYTACG
     GISPAYTLPL VLDVGTNNPQ LIDDPMYLGW RHPRISGDEY YRFVDDVMEA IKVRWPDALV
     QFEDFAQKNA MPVLERYRDK LCCFNDDIQG TAAVTVGSLL AACKAAGSAL HQQRIAFLGA
     GSAGCGIAEA IIAQMVAEGI SDSQARSQVY MVDRWGLLQD GMPNLLPFQQ KLTQSIESTG
     HWSDEEGNVS LLDVVKQGKP SVLIGVSGVP GLFTEQIIRE MHQHCSRPIV LPLSNPTSRV
     EATPAEILQW TQGEALVATG SPFSPVALGE QVFEIAQCNN SYIFPGIGLG ALACGAKRIT
     DNMLMAASRA LADTSPLAID GVGALLPPME DVQLVSRKIA FDVAIAAMAD GVATQISDDA
     LEQAIDDSFW KPEYRRYKRT SF
//
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