ID A0A0M2WQ01_9BURK Unreviewed; 1575 AA.
AC A0A0M2WQ01;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:KKO63780.1};
DE EC=1.4.1.2 {ECO:0000313|EMBL:KKO63780.1};
GN Name=gdhB {ECO:0000313|EMBL:KKO63780.1};
GN ORFNames=VM94_03533 {ECO:0000313|EMBL:KKO63780.1};
OS Janthinobacterium sp. KBS0711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1649647 {ECO:0000313|EMBL:KKO63780.1, ECO:0000313|Proteomes:UP000034315};
RN [1] {ECO:0000313|EMBL:KKO63780.1, ECO:0000313|Proteomes:UP000034315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS0711 {ECO:0000313|EMBL:KKO63780.1,
RC ECO:0000313|Proteomes:UP000034315};
RA Shoemaker W.R., Muscarella M.E., Lennon J.T.;
RT "Genome sequence of the soil bacterium Jantinobacterium sp. KBS0711.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKO63780.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LBCO01000024; KKO63780.1; -; Genomic_DNA.
DR RefSeq; WP_046684525.1; NZ_VCCE02000001.1.
DR PATRIC; fig|1649647.5.peg.3620; -.
DR Proteomes; UP000034315; Unassembled WGS sequence.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR048381; GDH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028971; NAD-GDH_cat.
DR InterPro; IPR049062; NAD_Glu_DH_ACT2.
DR InterPro; IPR049064; NAD_Glu_DH_ACT3.
DR InterPro; IPR007780; NAD_Glu_DH_bac.
DR InterPro; IPR049059; NAD_Glu_DH_HM1.
DR InterPro; IPR049056; NAD_Glu_DH_HM3.
DR InterPro; IPR024727; NAD_Glu_DH_N_ACT1.
DR PANTHER; PTHR43403; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR43403:SF1; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR Pfam; PF05088; Bac_GDH_CD; 1.
DR Pfam; PF21075; GDH_ACT1; 1.
DR Pfam; PF21076; GDH_ACT2; 1.
DR Pfam; PF21077; GDH_ACT3; 1.
DR Pfam; PF21074; GDH_C; 1.
DR Pfam; PF21073; GDH_HM1; 1.
DR Pfam; PF21078; GDH_HM3; 1.
DR PIRSF; PIRSF036761; GDH_Mll4104; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KKO63780.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034315}.
FT DOMAIN 33..166
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 390..476
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 543..600
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 703..1192
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1242..1386
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1575 AA; 169869 MW; 6859E20D7879D625 CRC64;
MNHTPQDLRT QTLELINAAG NAGKAAAPVV QLVQAWLDSL DAEDLADIAP DSLAPVLVEG
FTQAAKRTGS GCQIATLRYA DGRGGMASAL LILNEDMPYL VDSIVMAMRR QHLAVRGVMN
TVLPVRRAAD GSVEAVRQSG DPLESYVLVL LDEELAPEAL AALVAALETV ARDAAIVRRD
AAAMSERLAA VATAASQHGE EGAEVAAFLE WARSGGFEVF GYAYYRVKPG VRELERDIPS
RVGVLQDTAH PVYGTCLANI PGDFDTLAKR DSALSIVKAD VAGTLHRDQQ LDFIGVRDMD
AQGAILGEHC FVGLFTRAGN STPLAALPFA RGRVAKVLSL AGVRQQGFRA EKFREILESL
PRTEALEADL DWLAQVCGSV VSLYKQPRTK VFARRDVYAR HLNVLVYLPR ERYSASVASS
LAKALQASSG ATHVSMQTLV ADGPLARVYL IAHAARYPLD LETDIEQPLL SVLDGWHNGF
AAVADAVPDV ALRTSLRKLC ATLPLDYVAA TAPAVAFRDL DTILRNTDPS HVAVRIETGA
VTTIRLYSAN KVPPLSTILP ALHNAGVAID REQAYSVSLA DGTRYFVTSL TVDAASAAKL
AQPSVVAVAQ ELFASLFNDT AEDGRLNGLV IEGGLSTREV QLVRAYTSYW RQTGSRFSVR
YIAESLRKQP AQVKALVEAF LQRFDPSLSD AQHAQALESI AAIKAGLPSV NHADTEEILG
ALADLMAATL RTSYFQNNQQ GDKIIFKFDT SSLALVPEPR PYREIFVFSR RFEGVHLRGG
PVARGGLRWS DRMEDYRTEV LGLVKAQMVK NAVIVPAGAK GGFVCKMMPK DAVRETIAAE
GEAVYRLFIS SLLEVTDNRS LGNIVPPVDT VCFDEADPYL VVAADKGTAT FSDIANGIAV
QRGFWLGDAF ASGGSNGYDH KKLGITAKGA FEAVKRHFYE MDHDLNTTPI TMVGVGDMSG
DVFGNGVLLS RQLKLVAAFD HRHIFLDPTP DVAVSFEERA RLFALPRSSW DDYNKGLISA
GGGVYPRSAR TIELSPQIRA ALDIAETSLP PEELMHRILK SPVDLFYNGG IGTYIKASTE
THAQVKDRAN DHIRVSGNEL RVKVVAEGGN LGATQAGRIE FALAGGRIFT DAIDNSAGVD
CSDHEVNVKI WLDVEVNAGK LTEEERNREL YAMTDDVERL VLRDNTQQTH LLVRELQAQS
ESAVQDGYAA LIASLEEEGA LSRELEQLPS VAELARRKLD NRGLTTPELA VVIANVKNRF
KRILSALPLT GETWAEPVLK PYFPSLLVET RSALDHPLAN AILATVLANE VINRCGPLMI
RNLAAEHGVD ESSVILAWGQ AWVALNLAPV FDALDADALT IPRDVSIKVD AQTRVLQQTM
IAGVLSVPAE QLRGAGLAEL TRLFGAESKR ELLKAVGIKS EAVLVPGLTP AFVQAWDAVD
ALEVVAGFLF PALSVPRPAS MDLASFLQVG LALRSQAGID TLERGLKLAA QGKSQEQLRN
YAQQALRRTQ QRLLTQVLAR AEQGNAGQAV DAVTGALGLS AYVAATELEQ AMLDVWTLSE
AVNKITAKTP AEAAV
//