ID   A0A0N4Y7H8_NIPBR        Unreviewed;       883 AA.
AC   A0A0N4Y7H8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN   ORFNames=NBR_LOCUS12114 {ECO:0000313|EMBL:VDL75703.1};
OS   Nippostrongylus brasiliensis (Rat hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX   NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0001211301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:NBR_0001211301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL75703.1, ECO:0000313|Proteomes:UP000271162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
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DR   EMBL; UYSL01020677; VDL75703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4Y7H8; -.
DR   STRING; 27835.A0A0N4Y7H8; -.
DR   WBParaSite; NBR_0001211301-mRNA-1; NBR_0001211301-mRNA-1; NBR_0001211301.
DR   OMA; NDACANI; -.
DR   Proteomes; UP000038043; Unplaced.
DR   Proteomes; UP000271162; Unassembled WGS sequence.
DR   GO; GO:0004470; F:malic enzyme 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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR   Gene3D; 1.20.1370.30; -; 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; 2.
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; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR   PANTHER; PTHR23406:SF90; MALIC ENZYME-RELATED; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 3.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 2.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003426};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271162}.
FT   DOMAIN          2..172
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   DOMAIN          347..505
FT                   /note="Malic enzyme N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01274"
FT   DOMAIN          515..824
FT                   /note="Malic enzyme NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00919"
FT   REGION          217..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   883 AA;  99374 MW;  2F6F1C7368E591FB CRC64;
     MQRIVVQFSR CTSCYTNSAD APVVVGDGAS TVAGAFTEEV LREMSRINSR PIVFALSNPT
     SKAECTADAA YRISNGSVLF ASGSPFDNVE LNGKLYKPGQ GNNAYIFPGI ALGCVLFKAK
     HIPDKLFLLA ARRVAESVTE KSLYEYSRLY PRLKSIRELS IKIAVEVGDY LYKHNLATLH
     PRPEDMEMFI RQHVYSIEYQ ELINKTYDWP AKDAKHGFPT NPMGKDGEDP FAALKKMSPP
     SKEHCDKHHS HERNSKEFNL DDPQQKALHK LYRPEIVTPK YRGVELLKLP WLNKGLAFTL
     YERQFLGIHG LLPPAFMTAE QQACRVLKKL REQPDDLARY VQLDGLQDRN ERLFYRVLCD
     NIKELMRIVY TPTVGLACQK FGFIYRHPKY VAIVVTDGER ILGLGDLGAY GMGIPIGKLA
     LYVALGGVHP EWCLPILLDV GTDNEKLLKD PFYTGLRKKR IRGAPYDKLL DNFMIACTKR
     FGRNVLIQFE DFGNLNAYRL LDKYKKTFNM FNDDIQGTAA VVLAGLLTTM RITKKKLSEQ
     KFLFFGAGGA ATGVAEMCVR QMVEEGASVE EACENIYMVD IEGLLTKSRA ERLSPRHSAF
     AKDMEPTKDL LKVVKMVQPN ALIVFDDLAK ADLLAEHFAS VYSVHDDDSL ALGFQDLPVQ
     FSTMLDSVWF SKEEILETLG ASTVGGAFTD EIIKEMAEIN ERPIIFALSN PTSNAECTAK
     AAIQVTKGAV LFASGSPFEN VEYDGKTYKP GQGNNAYIFP GIGLGAVLFR SKHVTDKMFL
     NAARIVAESV TEKSLYTYSR LYPRLKDIRE ISIKIAIDAG HYLYHHGLAT LYPEPDDMEM
     YVRQHIYSCE YQDSVNRIYD WPEGDAKHGY PTPKLERLSM EDE
//