ID A0A158M6B8_9BORD Unreviewed; 498 AA.
AC A0A158M6B8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN ORFNames=L497_3452 {ECO:0000313|EMBL:KAK96139.1};
OS Bordetella holmesii CDC-H585-BH.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1331206 {ECO:0000313|EMBL:KAK96139.1, ECO:0000313|Proteomes:UP000026682};
RN [1] {ECO:0000313|EMBL:KAK96139.1, ECO:0000313|Proteomes:UP000026682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC-H585-BH {ECO:0000313|EMBL:KAK96139.1,
RC ECO:0000313|Proteomes:UP000026682};
RA Harvill E., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C., Cassiday P.,
RA Tondella M.L., Liao P., Zimmerman J., Meert K., Wessel D., Berger J.,
RA Dean J.M., Holubkov R., Burr J., Liu T., Brinkac L.M., Sanka R., Kim M.,
RA Losada L.;
RT "Genome sequence of Bordetella holmseii.";
RL Submitted (MAR-2014) 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|PIRNR:PIRNR000185,
CC 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:KAK96139.1}.
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DR EMBL; JFZZ01000044; KAK96139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158M6B8; -.
DR STRING; 35814.BBB42_01885; -.
DR PATRIC; fig|1331206.3.peg.1089; -.
DR Proteomes; UP000026682; Unassembled WGS sequence.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; 2.
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; IPR014362; Glu_DH.
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 PIRSF; PIRSF000185; Glu_DH; 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 NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185}.
FT DOMAIN 254..496
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-2"
FT SITE 218
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 498 AA; 54265 MW; 1CE11A219030D5CF CRC64;
MMSRAPLPEQ ANPPYNPRTK SVLFDGFAPF QIRRRTELIH QAPLCSITGG FFFMQSLNDF
LGRVASRDPH QPEFMQAVHE VMGSLWPFIE KNPHYGQQAL LERLVEPERV IQFRVCWTDD
KGRAQVNRAF RVQHSSAIGP FKGGMRFHPS VNLSVLKFLA FEQTLKNALT TLPMGGGKGG
SDFDPKGKSD GEVMRFCQAL MIELYRHLGP DTDVPAGDIG VGGREVGFMA GMMKKLSNSA
AAVFTGKGLT FGGSLIRPEA TGYGTVYFAE QMLHRVSMSF DGLRVSVSGS GNVAQYAVEK
AMALGARVLT VSDSGGTVLD EAGFTPEKLH ALMHIKNVQR GRVEDYAQQL GLRFLPGVRP
WQIPVDVALP CATQNELDEN DARTLIDNGV KCVAEGANMP ATLAAAQAFI DAHVLYAPGK
ASNAGGVAVS GLEMSQNSAR LSWTREDVDQ RLRAIMCDIH ENCVRHGHAE SGYVNYLDGA
NIAGFVKVAD AMLQQGLY
//
