ID Q5V4X6_HALMA Unreviewed; 427 AA.
AC Q5V4X6;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN Name=gdhA1 {ECO:0000313|EMBL:AAV45426.1};
GN OrderedLocusNames=rrnAC0384 {ECO:0000313|EMBL:AAV45426.1};
GN ORFNames=E6P14_20870 {ECO:0000313|EMBL:QCP93197.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV45426.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV45426.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:AAV45426.1}, and ATCC 43049 / DSM
RC 3752 / JCM 8966 / VKM B-1809 {ECO:0000313|Proteomes:UP000001169};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2] {ECO:0000313|EMBL:QCP93197.1, ECO:0000313|Proteomes:UP000298722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:QCP93197.1,
RC ECO:0000313|Proteomes:UP000298722};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) 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}.
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DR EMBL; AY596297; AAV45426.1; -; Genomic_DNA.
DR EMBL; CP039138; QCP93197.1; -; Genomic_DNA.
DR RefSeq; WP_004962147.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V4X6; -.
DR STRING; 272569.rrnAC0384; -.
DR PaxDb; 272569-rrnAC0384; -.
DR EnsemblBacteria; AAV45426; AAV45426; rrnAC0384.
DR GeneID; 64822752; -.
DR KEGG; hma:rrnAC0384; -.
DR PATRIC; fig|272569.17.peg.1165; -.
DR eggNOG; arCOG01352; Archaea.
DR HOGENOM; CLU_025763_1_2_2; -.
DR Proteomes; UP000001169; Chromosome I.
DR Proteomes; UP000298722; Chromosome.
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; cd01076; NAD_bind_1_Glu_DH; 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; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
DR NCBIfam; NF041398; GluDhGdhB_Halo; 1.
DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000185};
KW Reference proteome {ECO:0000313|Proteomes:UP000001169}.
FT DOMAIN 194..424
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00839"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-1"
FT SITE 157
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000185-3"
SQ SEQUENCE 427 AA; 46005 MW; CAF878397ECA222B CRC64;
MSTQKEPPEQ ATDEDESPIA TARRQLERAA EHLDLSEGML EQLRHPSKTV EVSVPIHRTD
GSVEVFNGYR VQHFEVRGPY KGGMRYHPSV SAEECTALAM LMTWKCAVMD LPFGGAKGGI
VVDPSTLDAQ ETEQLTRRFA EELREVVGPT KDIPAPDMGT DEQTVAWFMD AYSMQEGETV
PGIVTGKPTA VGGTHGREEA PGRSVAIVAR EALDYYDGSV EGATVAVQGF GAVGANAARL
LDSWGASVVA VSDVDGGIYD ESGLDIESIS ADGDEHGQLG AVDAPRQLSN AELLELDVDV
LIPAAVGNVL TEENAADVQA SIIVEGANGP TTTAADTVFE ERNIPVIPDI LANAGGVTVS
YFEWLQHINR RSWSREEVND ELEAEMLDAW EALQAEVEDR DVTWRTAAYI VALSRIGDAM
NARGLWP
//
