GenomeNet

Database: UniProt
Entry: A0A0K0Y9V8_9RHOB
LinkDB: A0A0K0Y9V8_9RHOB
Original site: A0A0K0Y9V8_9RHOB 
ID   A0A0K0Y9V8_9RHOB        Unreviewed;       751 AA.
AC   A0A0K0Y9V8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:SIO39557.1};
DE   SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:AKS47710.1};
DE            EC=1.1.1.40 {ECO:0000313|EMBL:AKS47710.1};
GN   Name=tme {ECO:0000313|EMBL:AKS47710.1};
GN   ORFNames=OSB_31970 {ECO:0000313|EMBL:AKS47710.1}, SAMN05444287_2633
GN   {ECO:0000313|EMBL:SIO39557.1};
OS   Octadecabacter temperatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=1458307 {ECO:0000313|EMBL:AKS47710.1, ECO:0000313|Proteomes:UP000067444};
RN   [1] {ECO:0000313|EMBL:AKS47710.1, ECO:0000313|Proteomes:UP000067444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB1 {ECO:0000313|EMBL:AKS47710.1,
RC   ECO:0000313|Proteomes:UP000067444};
RX   PubMed=26358607;
RA   Voget S., Billerbeck S., Simon M., Daniel R.;
RT   "Closed Genome Sequence of Octadecabacter temperatus SB1, the First
RT   Mesophilic Species of the Genus Octadecabacter.";
RL   Genome Announc. 3:e01051-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000184809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26878 {ECO:0000313|Proteomes:UP000184809};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SIO39557.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 26878 {ECO:0000313|EMBL:SIO39557.1};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC       family. {ECO:0000256|ARBA:ARBA00007686}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP012160; AKS47710.1; -; Genomic_DNA.
DR   EMBL; FSRP01000002; SIO39557.1; -; Genomic_DNA.
DR   RefSeq; WP_049835872.1; NZ_FSRP01000002.1.
DR   AlphaFoldDB; A0A0K0Y9V8; -.
DR   STRING; 1458307.OSB_31970; -.
DR   KEGG; otm:OSB_31970; -.
DR   PATRIC; fig|1458307.3.peg.3220; -.
DR   OrthoDB; 9805787at2; -.
DR   Proteomes; UP000067444; Chromosome.
DR   Proteomes; UP000184809; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
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-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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; 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; IPR045213; Malic_NAD-bd_bact_type.
DR   InterPro; IPR012188; ME_PTA.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR042113; P_AcTrfase_dom1.
DR   InterPro; IPR042112; P_AcTrfase_dom2.
DR   InterPro; IPR002505; PTA_PTB.
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   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF036684; ME_PTA; 1.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 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,
KW   ECO:0000256|PIRSR:PIRSR036684-2};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AKS47710.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067444}.
FT   DOMAIN          20..153
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          165..401
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   ACT_SITE        96
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         78..85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         138
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         139
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         164
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         289
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ   SEQUENCE   751 AA;  81190 MW;  4613B1014106A9BE CRC64;
     MADNRITRED ALAFHLDPTP GKWEIQATVP MTTQRDLSLA YSPGVAVPCE EIAENPELAY
     DYTNKGNLVA VISNGTAVLG LGNLGALGSK PVMEGKAVLF KRFADVNSID IELDTEDPDA
     FCAAVKLMGP TFGGINLEDI KAPECFIIEQ RLKEEMDIPV FHDDQHGTAV ICAAGLINAL
     HISGKKIEDV KIVLNGAGAA GIACIELLKS MGAKHEHCVV CDTKGVIYQG RTDGMNQWKS
     AHAIKTDLRT LEDAMKGADV FLGVSAKGAV TPEMVEDMAD NPVIFAMANP DPEITPEEAH
     AVRVDAIVAT GRSDYPNQVN NVLGFPYLFR GALDIHARAI NDEMKIACAR ALAQLAREDV
     PDEVAVAYGR KLTFGRDYII PTPFDPRLIH VIPPAVARAG MDTGVARRPI VDVEGYEESL
     KTRMDPTASI LRGINARARA NQHTIVFAEG DDPRILRAAV QYQRSGFGRA LVVGREDDVK
     AKLTAAGLGD AVRELRVVNA ANTSHLENYK EFLYERLQRK GHDRSDIHRM ASRDRHVFAA
     LMLAHGHADG MVTGATRKSA HVLEQINHVF DASPHDGVAG VTAVLSKGRI VLIADTLVHE
     WPDENDLADI AEQGAYVARR LGLEPRVAFI SFSTFGYPVS ERAEKMHMAP AVLDKRGVDF
     EYEGEMTVDV ALNTKAQEAY PFSRLTGPAN ILVVPARHSA SISVKLMQEM AGATVIGPIL
     AGIDKPIQIC STGATVNDIL NMAVLASSTS K
//
DBGET integrated database retrieval system