ID A0A0A0JIW5_9MICO Unreviewed; 1643 AA.
AC A0A0A0JIW5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:KGN37003.1};
GN ORFNames=N803_16435 {ECO:0000313|EMBL:KGN37003.1};
OS Knoellia subterranea KCTC 19937.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1385521 {ECO:0000313|EMBL:KGN37003.1, ECO:0000313|Proteomes:UP000030011};
RN [1] {ECO:0000313|EMBL:KGN37003.1, ECO:0000313|Proteomes:UP000030011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 19937 {ECO:0000313|EMBL:KGN37003.1,
RC ECO:0000313|Proteomes:UP000030011};
RA Zhu W., Wang G.;
RT "The genome sequence of Knoellia subterranea.";
RL Submitted (AUG-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:KGN37003.1}.
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DR EMBL; AVPK01000007; KGN37003.1; -; Genomic_DNA.
DR RefSeq; WP_035905907.1; NZ_AVPK01000007.1.
DR STRING; 1385521.N803_16435; -.
DR eggNOG; COG2902; Bacteria.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000030011; 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 Reference proteome {ECO:0000313|Proteomes:UP000030011}.
FT DOMAIN 33..178
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 409..501
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 559..627
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 741..1248
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1295..1636
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1643 AA; 181405 MW; F24942EC8CBA6F34 CRC64;
MTESSVHPRS TTLDSIVRAF AELDDRPDGA VVVSRYFRHV PEEELSARPA QTLAGSVKSH
LDLAQQRVPG TAAVRVFNPT TESDGWSSAR SVIQIVTDDM PFLVDSVTSA LVERDIDIHL
VVHPQLRVRR DASGALLETC DEDCVAPADG ADGVIAESWI LLTIDRESDE AGREELQAIL
ENVLVDVREA VADWPAMRTR CLVIAAELEG APPVGVPAEE VSQAVAFLRW MADNHFTFLG
YREYSLEETP DGDVIRPLPG SGLGMLQQDP PADKPLVPLS PESSRKAREQ GVLVLTKANS
RSTVHRPAYL DYVGVRTYSP DGQTLGEKRF LGLYASTAYT ESVLRLPVVA EKVAAVVERS
GLAADSHTGK DLIEVLETYP RDELIQASPD QLFETAMAVA QLQERRRTKL FLREDDFGRF
VSCQVYIPRD RYNTGVRTRM AAILKDAFGG ESVEFTARVS ERALSRLQFV VRMPAGEHIR
SLDEEQRADL ERRLVEVSRN WADRLGDGLR DRLGEVEGDR LFDRFGRGFP TAYEETFAVV
QGVADLHHLD RLGDDRRTSV ALYRPTDSPE NLRRFKLFRI DPLSLTDILP IFTDMGVEVV
DEQPYEVTRT DGSELHVYDF GLRVNDPEVW SGVTHERLRD LFESAVLAVW DGSAESDGFN
QLVLAARLTW RQVVILRTVA KYLRQTQATF SQSYFEDALV SNPGIATDLV AFFEARFDPD
AFSGTAGPQR DAAQAEIAER ITSALDDVSS LDEDRIIRAF LAVMQATLRT NFFQTVAAGA
ETDVDQDGVA DSKPYVSLKL NPKAIPDLPA PRPAYEIWVY SPQVEGVHLR FGSVARGGLR
WSDRREDFRT EILGLVKAQM VKNAVIVPTG SKGGFYAKQL PDPAVSREDW LAEGQSAYRT
FISGLLDLTD NRVGTEIQPP TRVVRHDEDD PYLVVAADKG TATFSDIANG VAQSYGFWLD
DAFASGGSAG YDHKAMGITA RGAWESVKRH FREMGVDTQT EDFTVVGVGD MSGDVFGNGM
LLSEHIRLVA AFDHRHVFVD PNPVAAQSFQ ERKRLFELPR SSWDDYDRSL ISEGGGVFAR
SLKSIAVTPQ MREALGLPEG VATMTPTELI HAIVLAPVDL FWNGGIGTYV KASSESHLEI
GDRANDAIRV NGDELRVQVV GEGGNLGLSQ LGRIEAALSG VRVNTDAIDN SAGVDTSDHE
VNIKILLGDV VRRGDLTVEE RNTLLASMTD DVAEHVLRDN YEQNVLLGNA RAQEVSMAPV
HQRLMGWLEE RGELDRGLEF LPTDAEIEKR TSEGIGLKSP EFAVLVAYAK LALKKDILES
ALPDDPYFAG TLADYFPAAL REAYAAELGD HPLRREIVTN SVVNSMVNRG GITFAFRAQE
EAAGSPEQVA RAFIVCREVF DLRGYVEEIE ALDNVLPTSV QTQLYLEFRR LLDRAVRWLL
AARPGQLDIT TEVERFAPVV ADLGPRIPEL LQGGERERVT AQVATWEEAG VPAGLAQRAA
SLLDSYSLLD VVDIATDLDH TPLEVAEVYF RMSERFSIDT MLNRVAALPR DDRWDSLARG
ALRDDLYGVL EAFTRSAFEF EEDLDGDGTV TADERIESWS RANADAIERG SGQLTGIRAL
EKPNSAALSV GLRALRSMVR SGK
//
