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Database: UniProt
Entry: Q0C5G7_HYPNA
LinkDB: Q0C5G7_HYPNA
Original site: Q0C5G7_HYPNA 
ID   Q0C5G7_HYPNA            Unreviewed;       755 AA.
AC   Q0C5G7;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   SubName: Full=NADP-dependent malic enzyme {ECO:0000313|EMBL:ABI76196.1};
DE            EC=1.1.1.40 {ECO:0000313|EMBL:ABI76196.1};
GN   Name=maeB {ECO:0000313|EMBL:ABI76196.1};
GN   OrderedLocusNames=HNE_0296 {ECO:0000313|EMBL:ABI76196.1};
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI76196.1, ECO:0000313|Proteomes:UP000001959};
RN   [1] {ECO:0000313|EMBL:ABI76196.1, ECO:0000313|Proteomes:UP000001959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI76196.1,
RC   ECO:0000313|Proteomes:UP000001959};
RX   PubMed=16980487; DOI=10.1128/JB.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA   Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA   Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA   Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA   Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA   Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(2006).
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; CP000158; ABI76196.1; -; Genomic_DNA.
DR   RefSeq; WP_011645326.1; NC_008358.1.
DR   AlphaFoldDB; Q0C5G7; -.
DR   STRING; 228405.HNE_0296; -.
DR   KEGG; hne:HNE_0296; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0281; Bacteria.
DR   HOGENOM; CLU_012366_0_0_5; -.
DR   Proteomes; UP000001959; 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; 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:ABI76196.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001959}.
FT   DOMAIN          22..155
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          167..404
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        98
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT   BINDING         80..87
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT   BINDING         140
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         141
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT   BINDING         166
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   755 AA;  81659 MW;  4D48680AD5A7FC4C CRC64;
     MTTQRPSFTD QEALDFHSHP TAGKISMVPT KPMGTQRDLS LAYSPGVAIP VLAIAENPDK
     AYDYTSKGNL VAVISNGTAI LGLGNLGPMA SKPVMEGKSV LFKRFADIDS FDVEVDTTDV
     EDFIRTVRNI GATWGGINLE DISSPACFII ESRLRDELDI PVFHDDQHGT AIIAAAGLIN
     ACHITGRQLK DTKVAISGAG AAGLSVAGLI RHLGVKAENI LICDTAGVVY EGRTEKMDQF
     KSAFAVKTAK RTLTEAMDGA DVFLGLSVKG AVTKEMVKSM AKNPIIFAMA NPDPEITPEE
     IKSVRSDAII ATGRSDYPNQ VNNVLGFPYI FRGALDVRAR GINEEMKVAC ARALAELARE
     DVPDEVAAAY HGARPSFGRE YIIPSPFDPR LISFVPPFVA QAAMDTGVAR KPIADMDNYR
     RSLIRRADPS AAFLQGLQAR ARETQRRIVF AEGEEPAVVR AAYSFKNQGL GHPILIGREA
     QVERAMEQMG IPLGSLDIIN ARLSDKNPVY VDFLYERLQR RGYLKRDVQR LVNQDRNIFG
     SCMLKNGDAD GMVTGVTRNY DAALKDAMLV LDPIAGQALI GMSMVINLGK TIFIADTSVH
     ELPDGPTLAN IALEAARAVR ALGFTPRVAF LSYSTFGNPM GERGDRVREA VAILDQRTDI
     DFEYEGDINA DVAMNPNHRM VYPFSRLSGP ANVLVMPAIH SASIATNLLE AMSRATVIGP
     MLFGLEKPVQ ISSLGATVGD IVDLATIAAY DTDNV
//
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