ID L7LJA2_9ACTN Unreviewed; 1532 AA.
AC L7LJA2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=NAD-dependent glutamate dehydrogenase {ECO:0000313|EMBL:GAC61210.1};
GN Name=gdh {ECO:0000313|EMBL:GAC61210.1};
GN ORFNames=GSI01S_15_00800 {ECO:0000313|EMBL:GAC61210.1};
OS Gordonia sihwensis NBRC 108236.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223544 {ECO:0000313|EMBL:GAC61210.1, ECO:0000313|Proteomes:UP000035083};
RN [1] {ECO:0000313|EMBL:GAC61210.1, ECO:0000313|Proteomes:UP000035083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108236 {ECO:0000313|EMBL:GAC61210.1,
RC ECO:0000313|Proteomes:UP000035083};
RA Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sihwensis NBRC 108236.";
RL Submitted (DEC-2012) 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:GAC61210.1}.
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DR EMBL; BANU01000015; GAC61210.1; -; Genomic_DNA.
DR RefSeq; WP_006896612.1; NZ_BANU01000015.1.
DR eggNOG; COG2902; Bacteria.
DR Proteomes; UP000035083; 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; 2.
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:UP000035083}.
FT DOMAIN 51..129
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 335..422
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 475..540
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 643..1147
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1195..1528
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
FT REGION 201..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1532 AA; 165650 MW; 4CC1891D4872F5BC CRC64;
MTVPFATEFA AYYFPDFSDG AAVASSAWDR LERHLRLGEV REPGETAVAT TDLPDGSIQI
QIVADDAPLL VESTLAVLDS RGLTIVANDH PVLAVRRDDQ GRIVGLDDVV VVGGDEAGAE
SWISVTTAPA SGVDGDELCA DVGAALTRAQ AVHADAAQIH RRLLSFADAL SADDEDADLL
SWFATRDNFL PVGARTAGGH AENGLGVWRD PDTDRPEPVA GEEPVGVDQV YLPTGLLRSR
FPIMVRVRLD GVEHQVVGTI TSIGLYQSVR SVPGVRGRVA DVLRGLGLSE DSYSGLAALE
LLQTYPLADL MAGDSAELTR RIGELLEAQT SRNPRFYART GPARGFASVL IFIPRETYST
AVRSRVVTLL EEELGGSRTE FLTRLSHSPL AQLQVLMRTD PEARHRVDDR LLDRLNEAVR
SWPDRVRAVR EADPEVARLL GTVSERYRDE RDPQDAAVDL PIAAGLAPGG LHVRLDRTDP
EAWRFVLYLA DQRAALTQIL PMLQSLGLTV LDEHPHVVDR PDGVQVAVYD FTVRPAPHVD
VAEAGDVDAR IAEAFSDMWL GVTEVDALGE LVLRAGLTSR TVAMIRAYAR YLNQCGVGFA
MTHVAAVLGN HRGVTNGLVE LFEASFDPDG AEPGRRDRAL EDLRARIAEI LSLDADRVVS
ALASAVEATL RTNFYADSGD PAAGIGPTIA MKLDTGAIPQ APQPRPKFEI YVYSPRVEGV
HLRFGDVARG GLRWSDRRED FRTEILGLVK AQAVKNAVIV PVGAKGGFVL RHPPVATGDA
AVDQSALREE GIACYRAFIA ALLQITDNLD PATGRVRPPA RVLRRDADDP YLVVAADKGT
ASFSDIANEV ADHYGFWLAD AFASGGSVGY DHKAMGITAR GAWESVKRHF REMGVDTQTQ
DFTVVGIGDM SGDVFGNGML LSRHIRLVAA FDHRHIFIDP DPVAATSYAE RARLFALPRS
TWDDYDRSLI SAGGGVWSRE QKSIDVTPQM RDALGLDDAV ERMSPPDLIR AVLLAPVDLL
FNGGIGTYVK ASDEADAEVG DKANDPIRVT GGQLRVRVVG EGGNLGVTQR GRIEADLAGV
RINSDALDNS AGVDCSDREV NIKVLLGSQI SAGVLDADDR NDLLLSMTDD VAELVLADNI
DQNAELGLAR DTAGEDVELH ARMLAHLAST GVDLELEALP TPEQLRRRRA GDLQRGLTSP
ELATMMAHVK LDAKSRLLES GLPDNDMFDA LASGYFPEPL RARFAAGIRT HRLRREIVTT
VLVNRIVADG GMTHLYALGE TSGTEVEDAT RATVVAMRVF GAAALLEELR TEQVSATTVD
DATRRIRNLL AAGSRWFLAH RPQPLAIAAE TTRYAQVADL GGRLDEWLTG TAERSVRERA
AALADSGVRP ALAQAVAISP YRLQLLDVLD IAEISDRSPD EVGELLFAVV ERFGIDELVS
QIAELGHADR WTQLARLSLR DEVFAVLRSL TRAILTMSEP EEPAAQKISD WSQARSAMIA
RTESTLADLA ATGRWDLATL SVAVRSLRSV VG
//
