ID A8UEM6_9FLAO Unreviewed; 760 AA.
AC A8UEM6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Bifunctional protein: malate dehydrogenase phosphotransacetylase {ECO:0000313|EMBL:EDP72453.1};
GN ORFNames=FBALC1_15167 {ECO:0000313|EMBL:EDP72453.1};
OS Flavobacteriales bacterium ALC-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP72453.1, ECO:0000313|Proteomes:UP000003630};
RN [1] {ECO:0000313|EMBL:EDP72453.1, ECO:0000313|Proteomes:UP000003630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALC-1 {ECO:0000313|EMBL:EDP72453.1,
RC ECO:0000313|Proteomes:UP000003630};
RA Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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 -!- 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:EDP72453.1}.
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DR EMBL; ABHI01000001; EDP72453.1; -; Genomic_DNA.
DR AlphaFoldDB; A8UEM6; -.
DR STRING; 391603.FBALC1_15167; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000003630; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000003630}.
FT DOMAIN 19..152
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 164..400
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 77..84
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 138
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 163
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 287
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 760 AA; 84090 MW; 9B34AC2D913CECC4 CRC64;
MSKQSKRIEA LVYHAKPTPG KIKVVPTKKY ASQRDLSLAY SPGVAEPCLE IEKEVDNVYK
YTAKGNLVAV ISNGTAVLGL GNIGPEASKP VMEGKGLLFK IFADIDVFDI EVDTEDVGAF
IETVKHIAPT FGGINLEDIK APEAFEIERR LKEELDIPVM HDDQHGTAII SAAALLNALE
LAKKKIGEVK IVVSGAGAAA ISCTRLYQSC GANRENIVML DSKGVIRKDR ENLTKQKAEF
ATHRTIDTLD EAMQDADVFI GLSMADIVTP AMLKSMAANP IVFAMANPNP EISYQLAVDT
RDDIIMATGR SDHPNQVNNV LGFPFIFRGA LDVRATKINE AMKMAAVKAL SKLAKEPVPE
QVNIAYAETR LTFGKDYIIP KPFDPRLIAE VPPAVAKAAM ESGVAKEPIE DWERYKNSLL
ERLGNDNKLV RMLLSRARTN PKRVVFAEAD QLDVLKAAQI VYDEGVGHPI LLGRKDTIIS
LMKEIDFDAD IPIIDPKSDE ELERKNRYAK AYWEKRKRQG VTIYSAEKKM RERNYYAAMM
VNEGDADTLI TGYSRSYPSV VKPMLELIGM ADGVSRVATT NVMMTQRGPM FLSDTSINIK
PNAKDLARIA RMTSRVTKMF GIEPVTAMIS YSNFGSSENP RAEKVKEAVS YLHKAYPDMI
VDGELQADFA LNPKMLQDIF PFSKLAGRKV NTLIFPNLDS ANITYKLLKE LNKAESIGPI
MMGMAKPVHI LQLDASVDEI VNMTAISVID AQEREKRQQK
//