ID L9U8R8_9GAMM Unreviewed; 590 AA.
AC L9U8R8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Malic enzyme, NAD-binding {ECO:0000313|EMBL:ELY21305.1};
GN ORFNames=HALTITAN_1960 {ECO:0000313|EMBL:ELY21305.1};
OS Halomonas titanicae BH1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1204738 {ECO:0000313|EMBL:ELY21305.1, ECO:0000313|Proteomes:UP000011651};
RN [1] {ECO:0000313|EMBL:ELY21305.1, ECO:0000313|Proteomes:UP000011651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH1 {ECO:0000313|EMBL:ELY21305.1,
RC ECO:0000313|Proteomes:UP000011651};
RX PubMed=23516210;
RA Sanchez-Porro C., de la Haba R.R., Cruz-Hernandez N., Gonzalez J.M.,
RA Reyes-Guirao C., Navarro-Sampedro L., Carballo M., Ventosa A.;
RT "Draft Genome of the Marine Gammaproteobacterium Halomonas titanicae.";
RL Genome Announc. 1:E0008313-E0008313(2013).
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, 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:ELY21305.1}.
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DR EMBL; AOPO01000007; ELY21305.1; -; Genomic_DNA.
DR AlphaFoldDB; L9U8R8; -.
DR PATRIC; fig|1204738.3.peg.2955; -.
DR Proteomes; UP000011651; Unassembled WGS sequence.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
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 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 PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; 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,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 110..290
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 300..556
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 133
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 275
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 276
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 299
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 487
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 590 AA; 65515 MW; D84A659D8D617184 CRC64;
MSQEHVTLRS NAANARCCCI AAVIDIKKRV LMTTESRRPL YLPYAGPSLL EMPLLNKGSA
FTQQERLAFN LIGLLPQKVE TIEDQLERVY RQYQQCHSDL EKHIHLRAIQ DDNETLYFRM
VSQHLEEMLP IIYTPTVGQA CQEFSNIYRN HRGLFISYPD REHMDDILRS ATKDNVKVIV
VTDGERILGL GDQGIGGMGI PIGKLALYTA CGGISPAYTL PIMIDVGTNN KALLDDPMYM
GWRHERVGQE EYDAFMAEFI AAVKRRWPNV LLQFEDFAQA NAVPLLERYR NELCCFNDDV
QGTASVVVGT LMAACQAREE TIAQQRVVFV GGGSAGCGIA EQVVVAMEAE GLTESEARSR
IYIVDRDGLM TSDQEWQRDF QRRLAHDPSL VAEWNGQGLE ETIAQIKPTV LIGVCGQRGI
FTEQVVRTMH AGCEHPVIMP LSNPTSQAEA VPEDVIRWTD GQALVATGSP FAPVVYNGRT
YPIAQCNNAY IFPGIGLGVI AASANRVTDE MLMSASRALA REAPLVKEGK GALLPPLSRI
RDISKSIAFE VAAQAQQNGV ALKTSGTTLR ELIEKASWSP DYRTYRRRAF
//
