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Database: UniProt
Entry: F9RF34_VIBSN
LinkDB: F9RF34_VIBSN
Original site: F9RF34_VIBSN 
ID   F9RF34_VIBSN            Unreviewed;       562 AA.
AC   F9RF34;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   28-MAR-2018, entry version 39.
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=VIBRN418_18023 {ECO:0000313|EMBL:EGU31719.1};
OS   Vibrio sp. (strain N418).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU31719.1, ECO:0000313|Proteomes:UP000003627};
RN   [1] {ECO:0000313|EMBL:EGU31719.1, ECO:0000313|Proteomes:UP000003627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N418 {ECO:0000313|EMBL:EGU31719.1,
RC   ECO:0000313|Proteomes:UP000003627};
RA   Strain E.A., Brown E., Allard M.W.;
RL   Submitted (AUG-2011) 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:EGU31719.1}.
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DR   EMBL; AFWD01000069; EGU31719.1; -; Genomic_DNA.
DR   RefSeq; WP_005596584.1; NZ_AFWD01000069.1.
DR   STRING; 701176.VIBRN418_18023; -.
DR   EnsemblBacteria; EGU31719; EGU31719; VIBRN418_18023.
DR   eggNOG; ENOG4107R1I; Bacteria.
DR   eggNOG; COG0281; LUCA.
DR   Proteomes; UP000003627; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003627};
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:EGU31719.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003627}.
FT   DOMAIN       78    258       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      268    528       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   COILED       47     67       {ECO:0000256|SAM:Coils}.
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;  61910 MW;  5A8500FF74554C12 CRC64;
     MYNDKRPLYI PFAGPALLST PLLNKGSAFS AQERISFNLE GLLPETTETI QEQVERAYQQ
     YRSFENDMDK HIYLRNIQDT NETLFYRLVQ NHISEMMPII YTPTVGAACE NFSNIYRRGR
     GLFVSYANRD RIDDILNNAS NHNVKVIVVT DGERILGLGD QGIGGMGIPI GKLALYTACG
     GISPAYTLPI VLDVGTNNPQ RLADPMYMGW RHPRITGADY DAFVEEFIQA VQRRWPEALV
     QFEDFAQKNA MPLLERYKNR ICCFNDDIQG TAAVTVGSLL AACKAAGSKL SDQRITFLGA
     GSAGCGIAEA IIAQMVSEGI SDAQARSQVY MVDRWGLLQE GMPNLLDFQQ RLVQPTENTA
     EWPNEGNGFS LLDVMANAKP TVLIGVSGAP GLFSKDVIKE MHKHCARPIV FPLSNPTSRV
     EATPNDIIRW TNGEALVATG SPFDPVVHDG KTYPIAQCNN SYIFPGIGLG VLAVSARRVT
     DEMLQESSRA LATCSPLAIN GQGALLPPLE AIHSVSKKIA FAVGKKAIEQ GVAQEITDEA
     LEEAIEAYFW QPVYRRYKRT AF
//
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