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Database: UniProt
Entry: A0A1B0VHW6_FERIS
LinkDB: A0A1B0VHW6_FERIS
Original site: A0A1B0VHW6_FERIS 
ID   A0A1B0VHW6_FERIS        Unreviewed;       373 AA.
AC   A0A1B0VHW6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:AMW32348.1};
GN   ORFNames=NA23_02925 {ECO:0000313|EMBL:AMW32348.1};
OS   Fervidobacterium islandicum.
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=2423 {ECO:0000313|EMBL:AMW32348.1, ECO:0000313|Proteomes:UP000093740};
RN   [1] {ECO:0000313|EMBL:AMW32348.1, ECO:0000313|Proteomes:UP000093740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AW-1 {ECO:0000313|EMBL:AMW32348.1,
RC   ECO:0000313|Proteomes:UP000093740};
RX   PubMed=26421103; DOI=10.1186/s40793-015-0063-4;
RA   Lee Y.J., Jeong H., Park G.S., Kwak Y., Lee S.J., Lee S.J., Park M.K.,
RA   Kim J.Y., Kang H.K., Shin J.H., Lee D.W.;
RT   "Genome sequence of a native-feather degrading extremely thermophilic
RT   Eubacterium, Fervidobacterium islandicum AW-1.";
RL   Stand. Genomic Sci. 10:71-71(2015).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|PIRSR:PIRSR000106-3};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785}.
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DR   EMBL; CP014334; AMW32348.1; -; Genomic_DNA.
DR   RefSeq; WP_033191161.1; NZ_CP014334.2.
DR   AlphaFoldDB; A0A1B0VHW6; -.
DR   STRING; 2423.NA23_02925; -.
DR   KEGG; fia:NA23_02925; -.
DR   eggNOG; COG0281; Bacteria.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000093740; Chromosome.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd05311; NAD_bind_2_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   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR045213; Malic_NAD-bd_bact_type.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR   PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
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.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   DOMAIN          11..143
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          155..371
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        31
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   ACT_SITE        86
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT   BINDING         128
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         129
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         154
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT   BINDING         279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ   SEQUENCE   373 AA;  40880 MW;  B924114D9CF782F1 CRC64;
     MRPLDIHKLL QGKYKITIPL EVTEENLKYL YTPGVAEVAL ECAKEPSNAF IYTRRKHVIA
     VVSDGSAVLG LGNIGPYGAL PVMEGKAMLF KEFGNLDAFP VCLGTQNTEE IISIVKALEP
     SFGGINLEDI SAPRCFEILK HLDSETSIPV FHDDQQGTAV VVLAGLQNAL KLAGKRISDV
     KIVVNGIGAA GYNITKLLLE YGAKNVYPCD VYGLLNESTA LHEYHLEISR LTNPKNISAT
     LKECLKDADV FIGVSKGNLL TGEDIKQMAK NPVIFALANP TPEIMPDTAY ENGAFIVATG
     RSDFPNQVNN LLAFPGIMRA AVEKQRKITH TILLKAAEII SKTVEPSRYM ILPKATDRRL
     HEMLYKGLIE IFD
//
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