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Database: UniProt
Entry: A0A328S627_9EURY
LinkDB: A0A328S627_9EURY
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ID   A0A328S627_9EURY        Unreviewed;       336 AA.
AC   A0A328S627;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:RAP45469.1};
DE   Flags: Fragment;
GN   ORFNames=BZ135_05910 {ECO:0000313|EMBL:RAP45469.1};
OS   Methanosphaera sp. rholeuAM6.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=1945580 {ECO:0000313|EMBL:RAP45469.1, ECO:0000313|Proteomes:UP000248984};
RN   [1] {ECO:0000313|EMBL:RAP45469.1, ECO:0000313|Proteomes:UP000248984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RholeuAM6 {ECO:0000313|EMBL:RAP45469.1};
RA   Hoedt E.C., Parks D.H., Rosewarne C.P., Denman S.E., Mcsweeney C.S.,
RA   O Cuiv P., Hugenholtz P., Tyson G.W., Morrison M.;
RT   "Culture- and metagenomics-based expansion of the genus Methanosphaera
RT   reveals their evolutionary depth and metabolic versatility.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|ARBA:ARBA00006382, ECO:0000256|RuleBase:RU004417}.
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:RAP45469.1}.
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DR   EMBL; MVAA01000083; RAP45469.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328S627; -.
DR   Proteomes; UP000248984; Unassembled WGS sequence.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05313; NAD_bind_2_Glu_DH; 1.
DR   Gene3D; 1.10.285.10; Glutamate Dehydrogenase, chain A, domain 3; 1.
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   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR033922; NAD_bind_Glu_DH.
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   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004417};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248984}.
FT   DOMAIN          94..334
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00839"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RAP45469.1"
SQ   SEQUENCE   336 AA;  36168 MW;  9A7FFE945F16B75E CRC64;
     FEQIFKNSLT GLPIGGGKGG SNFDPKGKSD REVMAFCQSF MNELYRHIGQ DQDVPAGDIG
     VGGREVGYLY GQYKRLTKQY EGVLTGKGLT FGGSLARTEA TGYGLLYFTN EVLKANGESL
     EGKTAVVSGS GNVATYAIEK AQQLGANVVT ASDSTGWVYD PEGIDVALLK DIKEVRRLRM
     SDYAAERPSA EYHEGKGVWT IEADVALPCA TQNEVDIDDA KNIVSNNYIA LVEGANMPTT
     LEATKYLQDN GILFGPAKAA NAGGVAVSAL EMSQNSERLS WTFEEVDNRL ANIMKNIFKQ
     IQDSCTKYEQ GNDYVAGANI AGFEKVAEAM QGQGIV
//
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