ID A0A1R4HJV1_9GAMM Unreviewed; 770 AA.
AC A0A1R4HJV1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative fused malic enzyme oxidoreductase putative phosphotransacetylase {ECO:0000313|EMBL:SJM96505.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:SJM96505.1};
DE EC=2.3.1.8 {ECO:0000313|EMBL:SJM96505.1};
GN Name=maeB {ECO:0000313|EMBL:SJM96505.1};
GN ORFNames=CRENPOLYSF1_900012 {ECO:0000313|EMBL:SJM96505.1};
OS Crenothrix polyspora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Crenotrichaceae; Crenothrix.
OX NCBI_TaxID=360316 {ECO:0000313|EMBL:SJM96505.1, ECO:0000313|Proteomes:UP000195667};
RN [1] {ECO:0000313|EMBL:SJM96505.1, ECO:0000313|Proteomes:UP000195667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSM_CP1 {ECO:0000313|EMBL:SJM96505.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUKI01000171; SJM96505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4HJV1; -.
DR OrthoDB; 9808984at2; -.
DR Proteomes; UP000195667; Unassembled WGS sequence.
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:0008959; F:phosphate acetyltransferase 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; IPR032683; Malate_DH.
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; PF12434; Malate_DH; 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 Acyltransferase {ECO:0000313|EMBL:SJM96505.1};
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:SJM96505.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195667};
KW Transferase {ECO:0000313|EMBL:SJM96505.1}.
FT DOMAIN 28..161
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 173..410
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 86..93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 147
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 297
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 770 AA; 83851 MW; 93E013EB6BE36F4A CRC64;
MTSSPDPKEN QHLSLREAAL EYHQFPTPGK ISVTPTKHLT NQRDLALAYS PGVAAACDEI
VIDPANVFKY TARGNLVGVV TNGTAVLGLG NIGPLASKPV MEGKAVLFKK FAGIDVFDLE
INEPDPDRLC DIIAALEPTF GGINLEDIKA PECFYIERKL SERMKIPVFH DDQHGTAIIV
AAALLNGLKV VGKDLKHCKL VVSGAGAAAL ACLNLLVELG FPIDNIFVTD LAGVVYQGRI
ELMDPDKARF AQATDARSLA EVIKNADIFL GLSAGGVLKQ DMVKRMADRP LIFALANPTP
EILPEEIKAV RDDAVIATGR SDYPNQVNNV LCFPYIFRGA LDCGATTVNL AMKMAAVQAI
ADLAQAEQSD VVAKTYGVSN LSFGADYLIP MPFDPRLMTK IAPAIAKAAQ DSGVATRPIV
DMQAYIEHLQ QFAYHSGTFM RPIFQLTKHV EAAKKRIVFA EGEEENILRA LQIIVDEKIA
NPILIGRPAI LERRIKKFGL RLKPGIDFQI VNPEHDERYR DYWQTYLQMT IRKGVTEQYA
KLEMRRRHTL IGAMMVHKGD ADGMICGTFG ATGLHLHYIN HVLGKRPGVN VYAAMNVLIL
PERQIALVDT HINENPTAEQ LAEITLLAAE QMRRFGLIPR VALLSHSNFG SGSTESAQKM
RDTLALLQTQ APNLEVDGEM HGDTALDFDI LKQLMPNSPL QGSANLLVLP TIDAANIAYN
LLKVAAGNGI AIGPVLLGCA KPVHILTQSA TVRRIVNMTA LCVLDAVEAR
//
