ID Q0FDI9_9RHOB Unreviewed; 758 AA.
AC Q0FDI9;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Malic enzyme {ECO:0000313|EMBL:EAU52505.1};
DE EC=1.1.1.39 {ECO:0000313|EMBL:EAU52505.1};
GN ORFNames=OM2255_10126 {ECO:0000313|EMBL:EAU52505.1};
OS Rhodobacterales bacterium HTCC2255.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU52505.1, ECO:0000313|Proteomes:UP000009381};
RN [1] {ECO:0000313|EMBL:EAU52505.1, ECO:0000313|Proteomes:UP000009381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU52505.1,
RC ECO:0000313|Proteomes:UP000009381};
RA Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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:EAU52505.1}.
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DR EMBL; AATR01000002; EAU52505.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0FDI9; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OrthoDB; 9805787at2; -.
DR BioCyc; RBAC367336:G1GNW-1466-MONOMER; -.
DR Proteomes; UP000009381; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) 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: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; 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.
PE 3: Inferred from homology;
KW Metal-binding {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:EAU52505.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009381}.
FT DOMAIN 23..156
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 168..404
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 81..88
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 167
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 291
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 758 AA; 81904 MW; 580D9D3217159998 CRC64;
MAKETKKSIE KQAALDYHEF PRAGKLEIRA TKPMANGRDL SRAYSPGVAE ACLEIEKNPD
DARRYTSRGN LVAVISNGTA VLGLGDIGAL ASKPVMEGKA VLFKKFAGID CFDIEVNEPD
PKKLAEIVCS LEPTFGAVNL EDIKAPDCFI VEKICREKMG IPVFHDDQHG TAIVAAAAAS
NALIVAKKSF SDIKIVALGA GAAGIACLKM MMVMGAKKEN ITMIDSKGVV HTQRNDLTAE
KSEFARNTTK RTTMEAMEGA DLFLGVSGPG LLTQEMVKKM ASHPIIFALA NPTPEIMPEE
AREASADALI ATGRSDYPNQ VNNVLCFPFI FRGALDVGAT TINDEMKAAC VEAIAGLARE
TASAELGAAY QGERLAFGPD YLIPKPFDPR LLPTIAYAVA KAAIDSGVAK NKLDLDAYHA
KLQTQVYRSA VTMRPIFEAA KTDNRRVVFA EGEDVKVLRT VQAMSEELSE TAVLIGRPNV
IESRIEREGL SIKAGVDFEL VNPEKDTRYR DYWQSYHDIM ARKSITPDLA KAIMRTNTTA
IAAVMVHRGE ADSMICGTFG QYHWHLKYIK QVLANQDLTP VGALSLVILD QGPLFIADTH
VNIEPSAQQI ANTMIAAARH TRRFGIEPKL ALCSSSQFGN ADTHSGRVTR EALAILDSHK
VDFEYEGEMH TDAALDEDLR ETMMPNNRLK GKANILVYAN SDAAGATRNV LKSVAGGLEV
GPILMGMGNR AHIVTPGVTV RGLLNIAALA GSPVSSYE
//
