ID V2XRE3_MONRO Unreviewed; 609 AA.
AC V2XRE3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Nadp-specific glutamate dehydrogenase {ECO:0000313|EMBL:ESK82029.1};
GN ORFNames=Moror_13449 {ECO:0000313|EMBL:ESK82029.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK82029.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK82029.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK82029.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000256|ARBA:ARBA00006382}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESK82029.1}.
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DR EMBL; AWSO01002105; ESK82029.1; -; Genomic_DNA.
DR RefSeq; XP_007858667.1; XM_007860476.1.
DR AlphaFoldDB; V2XRE3; -.
DR STRING; 1381753.V2XRE3; -.
DR KEGG; mrr:Moror_13449; -.
DR HOGENOM; CLU_000384_30_3_1; -.
DR OrthoDB; 1608098at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005162; Retrotrans_gag_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR43571; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR43571:SF1; NADP-SPECIFIC GLUTAMATE DEHYDROGENASE 1-RELATED; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR Pfam; PF03732; Retrotrans_gag; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 548..561
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 271..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 68136 MW; 6ED739F0E46645EC CRC64;
MGGGKGGSDF DPKGKSDAEI RRFCVAFMSE LSKHIGQDTD VPAGDIGTRG REIGFLFGAY
KKLRNEFTGV EASSDQRLRV MESSTTLSIL NKPSTLVAIS GSGNVSQYTA LKVIKLGATV
VSLSDSKGSL IATTEKGFSK ENLLPMKSKR PWTLLPEIHT ALPGATENEV SGEEAEALIA
AGTRIVAEGS NMGCTPEAIE NPKIGISCPG KGKRRIVTTD NQNTQNQEQN QTRPRLQNRL
RAIQGRKENI DPNFFPTIAA AFTGMDELPD YRDKTDRPED NILTTSSSTP PPRIPNMTMQ
QTGTSLQDLI TALRTLQSNG EKKKENKVAV LNSYNGSPSK ASTFLTEVDL FLMANETIYP
NDKDKILFTL SYMKDGHATK WMKAKAKEYK QTLLEKEAET TDTKPEEQVH VMTWEEFLSD
FKKAFQPINV GTNACLKMKQ LKQNKRTVDE YISDFCLLAL DSEYDDRALI DHFMTGLHPA
LLKACLMVPD HPDTIEGWYN RARKYNSNWL MTMAITRGER TKKSPQTEKR VNHILDEESA
KYQKKGLCYR CSKPGHIAKN CLEKQDNEQK KKPNKATPRD VYHQIHAIYR DFSEDEQTQI
LGFMEGEGF
//
