ID B2JR70_PARP8 Unreviewed; 1634 AA.
AC B2JR70;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:ACC73736.1};
GN OrderedLocusNames=Bphy_4626 {ECO:0000313|EMBL:ACC73736.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC73736.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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DR EMBL; CP001044; ACC73736.1; -; Genomic_DNA.
DR STRING; 391038.Bphy_4626; -.
DR KEGG; bph:Bphy_4626; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_4; -.
DR Proteomes; UP000001192; Chromosome 2.
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; IPR049058; NAD_Glu_DH_HM2.
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; PF21079; GDH_HM2; 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 Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT DOMAIN 52..196
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 423..512
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 568..646
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 744..1238
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1283..1624
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1634 AA; 181870 MW; 7AF2575804FD775C CRC64;
MRFSRCSRLS PQAEDVMQAK NEEAVAHLLN DVVEFARGRL PEPAFAAVEP LLRHYYDFAD
ADDLQSRGIA DLYGAAMAHW QTAQRFVPGS ERLRVYNPIL EQHGWHSDHT VIEIVNDDMP
FLVDSVAMAV NRQGLALHSV LHPVFRIWRG KDGGIERIAP GGASSDDGQS QLASFIHFEV
DRFGDAAKLD VLRNEIAKVL GDVRAAVEDW PKIVEIARTT IHDMAARETS PEGVEARAFL
EWMVADHFTF LGQRDYELVS HDGQYGFRGL AGSGLGILRE SSRPQGASDV TPLPPAAADI
IAGAAPIFLT KANSRATVHR PGYLDYVGVK LVGPDGKISG ERRFIGLYTS TAYTASASEI
PIVRRKCANI VRRAGFLPKG HLGKSLVTVL EMYPRDELFQ ADENELYDTA MGVLRLQEHQ
RTRIFLRRDR FDRFVSCLVF VPRDKYNTDL RRRIAKLLMS AFNGTNVEFT PLLSESTLAR
IHFVVHAEPG AMPDVDMREL EARLIQVSRR WQDDLADALL DAFGEEQGNR LLQHYADSFP
AGYRDDYPAR TAVRDIELIE RVQGTGHIAM NLYRPIEAGP RAFRFKVYRV GEPIALSRSL
PMLEHLGVRV DEERPYLIET PGAAPAWIHD FGLELADDSE FDIERVKGLF EDAFDRVWTG
DIEDDNFNRL VLRAQLSARE VTILRAYAKY LRQVGSTFSD AYIERALTGN PAIARMLVEL
FVARSDPAPA TSRDTRVERL LKTIESALDE VPNLDEDRIL RQFLGVINAT QRTNYYRREP
NGKPRPYLSF KFDPAKVPGL PEPRPMFEIW VYSPRVEGVH LRGGRVARGG LRWSDRREDF
RTEVLGLMKA QMVKNVVIVP VGSKGGFVVK NPPPPTDREV WMREGVACYQ TFLRGLLDLT
DNRVGGQIVP PPDVVRHDPD DPYLVVAADK GTATFSDYAN AISQEYGFWL DDAFASGGSV
GYDHKKMGIT ARGAWESVKR HFREMGVDTQ TTDFTVVGVG DMSGDVFGNG MLLSQHIRLI
AAFDHRHVFL DPNPDPATSF AERQRLFSLD RSSWADYDPA LISAGGGVFA RTAKTIPLSQ
AVQSMLGINA PALSPAELVR AILQAPVDLL YNGGIGTYVK ASRETHAQVG DKTNDAVRVN
GCDLRCKVVA EGGNLGFTQH GRIEFAQHGG RMNTDAIDNS AGVDCSDHEV NIKILLGLVV
ADGEMTEKQR NALLAEMTEE VGLLVLQDNY YQTQALSIAG RYAAELFDAE MRMMRYLERA
GRLNRVIEFL PSEDEINERL AAKQGLTSPE RAVLLAYSKM WLYDALLESD VPEDALVSGM
LTEYFPKPLR QRFNEPMHRH PLRREILATH LTNALVNRVG CAFVHRMMEE TDAKPGDIVR
ACIIARDVFD LNDVWRNIDA LDNRVADDVQ ASMFVEITKL LERAALWFLR HLQSGEVTNG
GVTALIARCR DAAQRLAPQL PMLLPAAELE ALSERQRVLV DAGVDSELAV RVASGDIPAA
LLDIADVSAT TDRSLELVAG VYFALSTQLN YGWIGERAAS LPTSTHWDVM ARAAALAELA
RLKRVLTTSA LTEAREATTA EGVVETWRAK REDALARYAQ LLTDLRAAGG ASLSMLLVIV
REMATLERRQ VSAS
//
