ID S9ZHU1_9RHOO Unreviewed; 1606 AA.
AC S9ZHU1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:EPZ16970.1};
GN ORFNames=M622_09555 {ECO:0000313|EMBL:EPZ16970.1};
OS Thauera terpenica 58Eu.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=1348657 {ECO:0000313|EMBL:EPZ16970.1, ECO:0000313|Proteomes:UP000015455};
RN [1] {ECO:0000313|EMBL:EPZ16970.1, ECO:0000313|Proteomes:UP000015455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=58Eu {ECO:0000313|EMBL:EPZ16970.1,
RC ECO:0000313|Proteomes:UP000015455};
RA Liu B., Frostegard A.H., Shapleigh J.P.;
RT "Draft genome sequence of Thauera terpenica.";
RL Submitted (JUN-2013) 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:EPZ16970.1}.
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; ATJV01000013; EPZ16970.1; -; Genomic_DNA.
DR RefSeq; WP_021247896.1; NZ_ATJV01000013.1.
DR STRING; 1348657.M622_09555; -.
DR PATRIC; fig|1348657.5.peg.442; -.
DR eggNOG; COG2902; Bacteria.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000015455; 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; 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:UP000015455}.
FT DOMAIN 35..176
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 406..495
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 550..628
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 726..1221
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1268..1603
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1606 AA; 178285 MW; 62EE46F3BCC4914F CRC64;
MEKTELKRLA VQVDAVIEQI DARLPAHQAG AVAEFAAQFF AQVDPEDLEK LSVADLYGAV
LSQWHFIARR KSGVSTVRVF NPRLDEHGWE SAHTLVEIVG DDMPFLVDTV TMELIRQGFT
LHLLIHPVLK VVRDADGVLL RLTDDSDADA QYESTMHLEV DRRSDEADLQ ALQQGLEQVL
SDVRAAVSDW RLMRERMHDI IAGLLSTPAS IEAEEAAEAR DFLQWLTADN FVLLGCRDYA
LASAEDGDAL HIVSGSGLGL LRAEGEDGQS RSFAALPPQL RAQAHVPGVL TVTKSNTRST
VHRPGYLDFI GVKTFDSEGR VSGERRVIGL LASTAYGTSP AHIPLLRRKV AAVIERADLP
SGGHAAKTLQ TIIERYPRDE LFQITIDELY TQAMGILRLG ERLRTRLFVR CDPFARFVSC
LIYVPREHYN TDQRQRMQAV LVEAFDGSSS EFDVQFSDSA LARIQIIVRT RDSVIPPFDV
RELEQRLIRA SRPWEDALRQ ALVEQCGEER GLALLRRYGK GFPAGYREDY SARMAVFDIE
QIEGLGGVGE LGMNLYRPLE GAADRINFRI YHLDASVPLS QSLPMLERMG VKVMDERPSE
IVRQDGSVVW LHDFGLSFSA AETLNIHDIQ PLFHDTFRRV WSGEVENDDF NRLVLLAGLS
WREVSVLRAY AKHMRQAAFT FSQAYMEQAL ACYPQLTRQL YALFRARFDP ALEADREAHC
KDITAQIEAS LNTVANLDED RILRQFLAMI LATLRTNAFQ RTADGSCKPW LSFKLSPARI
PNLPQPLPMF EIFVYSPRIE GVHLRGGKVA RGGLRWSDRM EDFRTEVLGL VKAQIVKNAV
IVPVGSKGGF VVKNPPTEGG REALIAEGVA CYQTFLRGLL DLTDNLVQGQ VVPPVDVVRH
DDDDPYLVVA ADKGTASFSD HANEISAEYD FWLGDAFASG GSVGYDHKKM GITARGAWEA
VKRHFREMGT DIQNQPFTVA GIGDMSGDVF GNGMLLSKHI RLVAAFDHRH IFIDPEPDAA
RSWEERARLF ALPRSSWDDY DKALISEGGG VWARSAKSIK LSPQLRAVLD IEAEALAPVE
LIRAILCAPV DLVYNGGIGT YIKAASEADA AVGDRANDAV RVNGGALRCK VLGEGGNLGA
TQLGRIEFAL KGGRVNTDAI DNSGGVDCSD HEVNIKILLN GVVAEGELTL KQRNQLLADM
TDEVAALVLR DNYAQTQILA LTRLRGVALL DEQAEFMRRL SHLGRLSRKL EFLPVDEDLA
ERKAARIGLT NPELAVLLAY SKIELYDEVL ASDVPEDPYI STALERYFPA PLRTRFGAQI
QHHALRREII STHVVNSMVN RVGPTFAGRL KSEQGVRAPD VVRAYMATRE VFGLVDVWAQ
IEALDNQLDH AVQVDLMSAC DRLVQRGSLW FLRHPEWLSD LQATLHHFSP GVAALAGDLL
ALVGDAYRSE LEATVRRAVD QGVPQALAER VAALDELYSA LDLVEIAVET QRPEPFVARV
YFGLGGDLEL HWLGQQISAL ATENRWQVLA RGALRSDLSA LARSLTTNAL QLTVDEDDAQ
QVMAAWYQRQ GARLERYRQL LGDMRSAQSV DLAMVSVLLR ELRGMS
//
