ID A0A0F5EZV6_AVIPA Unreviewed; 756 AA.
AC A0A0F5EZV6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:SUU98074.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:SUU98074.1};
GN Name=maeB {ECO:0000313|EMBL:SUU98074.1};
GN ORFNames=EIG79_01385 {ECO:0000313|EMBL:RZN61183.1}, NCTC10926_01482
GN {ECO:0000313|EMBL:SUU98074.1};
OS Avibacterium paragallinarum (Haemophilus gallinarum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Avibacterium.
OX NCBI_TaxID=728 {ECO:0000313|EMBL:SUU98074.1, ECO:0000313|Proteomes:UP000254620};
RN [1] {ECO:0000313|EMBL:SUU98074.1, ECO:0000313|Proteomes:UP000254620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10926 {ECO:0000313|EMBL:SUU98074.1,
RC ECO:0000313|Proteomes:UP000254620};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RZN61183.1, ECO:0000313|Proteomes:UP000294229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-3 {ECO:0000313|EMBL:RZN61183.1,
RC ECO:0000313|Proteomes:UP000294229};
RA Hellmuth J.E., Boucher C.E., Cason E.D.;
RT "Sequencing Av. paragallinarum serogroups.";
RL Submitted (NOV-2018) 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}.
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DR EMBL; RQXS01000003; RZN61183.1; -; Genomic_DNA.
DR EMBL; UFSW01000001; SUU98074.1; -; Genomic_DNA.
DR RefSeq; WP_046098332.1; NZ_VXDA01000056.1.
DR AlphaFoldDB; A0A0F5EZV6; -.
DR STRING; 728.VY92_01060; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000254620; Unassembled WGS sequence.
DR Proteomes; UP000294229; 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:SUU98074.1}.
FT DOMAIN 18..151
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 163..401
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 76..83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 136
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 288
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 756 AA; 81801 MW; F329E31937F1E25B CRC64;
MDAQLRQAAL DFHEFPKPGK IEVTPTKSLA TQRDLALAYS PGVAEPCLEI EKDPSTAYKY
TARGNLVAVI SNGTAVLGLG NIGALAGKPV MEGKGVLFKK FAGVDVFDIE IDEKDPDKLV
DIIAALEPTF GGINLEDIKA PECFYIEQKL RERMKIPVFH DDQHGTAIIS AAAVINGLRI
VNKKIEDVKL VASGAGAASI ACLNLLVSLG MKKEHITVCD SKGVIFKGRD ERMDETKKLY
AIEDNGTRTL ADAMPNYDIF LGCSAAGALT QEMVKTMARD PLILALANPE PEILPPLAKA
VRPDAIVCTG RSDYPNQVNN VLCFPFIFRG ALDVSATTIN EEMKLAAVYA IADLALAEQS
EVVTSAYGGA EVSFGPDYLI PKPFDPRLIV KIAPAVAKAA MDSGVATRPI EDFDAYLEKL
TQFVYKTNLF MKPVFAQAKQ DKKRVLLTDG EETRVLHAVQ EIATLGIAQP VLLGRTHIIA
EKIKKLGLHL EAGRDFDIID IENNPHYEQC WQSYYNKLKR QGMTPAGAKR KMLHNPTALG
SVLLELGKAD AMLCGLVGPY PSHLNAIKEF NGVKAGAIPA TVNGLVLPTG NLFIADTFVN
PNPTAEELAE ITLMSAEEVR RFGIEPQVAL VSHSNYGSAN DENAVKMRQV LKLVQEKAPD
LIIDGEMHCD IALSESLRKE IMPDSPLKGA ANLLIMPTME AARISLNLLQ GTATPITIGP
ILMGVNKTAH ILTSASSVRR IINMVAIAAV KAQQER
//