ID Q3JAT5_NITOC Unreviewed; 783 AA.
AC Q3JAT5;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Allosteric NADP-dependent malic enzyme {ECO:0000313|EMBL:ABA58061.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:ABA58061.1};
GN OrderedLocusNames=Noc_1582 {ECO:0000313|EMBL:ABA58061.1};
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261 {ECO:0000313|EMBL:ABA58061.1, ECO:0000313|Proteomes:UP000006838};
RN [1] {ECO:0000313|Proteomes:UP000006838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107
RC {ECO:0000313|Proteomes:UP000006838};
RX PubMed=16957257; DOI=10.1128/AEM.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
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}.
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DR EMBL; CP000127; ABA58061.1; -; Genomic_DNA.
DR RefSeq; WP_002808659.1; NC_007484.1.
DR AlphaFoldDB; Q3JAT5; -.
DR STRING; 323261.Noc_1582; -.
DR KEGG; noc:Noc_1582; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_012366_1_1_6; -.
DR InParanoid; Q3JAT5; -.
DR Proteomes; UP000006838; Chromosome.
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; 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:ABA58061.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006838}.
FT DOMAIN 16..149
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 161..404
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT REGION 442..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 74..81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 134
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 135
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 160
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 783 AA; 85664 MW; 348D2DEEFFDCA214 CRC64;
MIFRDEALEY HRRGRAGKLE VIPSKPCLTQ HDLALAYSPG VAEPCREIHR SPDDVYLYTG
KGNLVAVVTN GTAVLGLGPL GPLASKPVME GKGVLFKRFA DIDVFDIELN APTAEEVIQA
CQLLEPTFGG INLEDIAAPD CFHIEERLRE TLTIPVFHDD QHGTAIISGA ALLNACELAG
KRLEDIKLVM NGAGAASIAC AKFYLTLGVD PDNLLLCDSK GVLYKGREDL MPGRPRYNEY
KAQFIRPTRL RTLPEALAGA DAFCGLSVAN VVTPDMVRSM NDNPIIFALA NPDPEITYPD
ALAARPDVIM ATGRSDYPNQ VNNVLGFPFI FRGALDVRAR AINEAMKVAA AQALAALAKE
GVPESVCRAY GMERIEFGRE YLIPKPFDPQ VLLEVTTAVA KAAGESGVAR VPIRDFRAYR
EQLERRLGRS KEVMRQVINK ARRRSQLSTQ HLESKTSPVE KPVSPGPLRI AFPEGDDKRI
IRAAARIVKE GIGKPVLLGK PDEIQALAKQ LSVNLEGIDL LDSQTHPQRE DLAQQFFAMR
ARKGVTLAEA RRYMLRRHYY APMLLLQGEV EAVVCGETYH YPDSIRPALQ ILPLAKGISH
ASGLYMLLFK NRLIFCADTT VNITPDAETL AEIALSAADT AHHFDIEPRV ALLSFSNFGS
VKHSLVDLVQ AAVKILHRRR PDLVVDGEMQ ADTATNEDIL SSTYPFSRLK EDANVLIFPD
LTSGNIAYKL LVELGGAEAI GPILTGLSKP YHVLQRDASV DAIVNIAAIA AVQAQEIELS
QQA
//
