ID D7BVP8_STRBB Unreviewed; 1663 AA.
AC D7BVP8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:ADI09627.1};
GN OrderedLocusNames=SBI_06507 {ECO:0000313|EMBL:ADI09627.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI09627.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI09627.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI09627.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
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; CP002047; ADI09627.1; -; Genomic_DNA.
DR RefSeq; WP_014179077.1; NC_016582.1.
DR STRING; 749414.SBI_06507; -.
DR KEGG; sbh:SBI_06507; -.
DR PATRIC; fig|749414.3.peg.6704; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_11; -.
DR Proteomes; UP000000377; Chromosome.
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:UP000000377}.
FT DOMAIN 43..191
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 449..542
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 600..670
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 777..1274
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1319..1656
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1663 AA; 185266 MW; 6CAD9C64C5F42F0A CRC64;
MQTKLDEAKA ELLTRAARVA ESSPAGGQQP VQGPGPETLT AYLQHYYQHT PPEDLAGRDP
VDVFGAALSH YRLAESRPQG TANVRVHTPT VEEHGWTCSH SVVEVVTDDM PFLVDSVTNE
LTRQGRGIHV VIHPQILVRR DITGKLIEVL DVVPDGRPEK LPHDAVIESW IHVEIDRETD
RGDLKQITAD LLRVLSDVRE AVEDWEKMRE AALRIAEGLP EEPTAGEVRP QEIEEARELL
RWLADDHFTF IGFREYELTQ APTESGGEED VLSAVPGTGL GILRSDPHHR DTDESAHAGL
PAAADGAAGR PVSPSFNRLP ADARAKAREH KLLVLTKANS RATVHRPSYL DYIGVKKFDA
KGNVIGERRF LGLFSSAAYT ESVRRVPVIR RKVEEVLEGA GFQPNSHDGR DLLQILETYP
RDELFQTPVD QLRSIVTSVL YLQERRRLRL FLRQDEYGRY YSALVYLPRD RFTTEVRLRL
TDILLEELNG RVPVDFTALH TESVLSRLHF VVRVQSGTEL PDLTDADVER IEARLVEAAR
SWADGFAEAL TSEVGEERAA ELLRRYQHAF PEGYKADHSP RGAVADLQNL ERVKDSDRNF
AVSLYEPVGA APAERRFKIY RVGEQVSLSA VLPVLTRLGV EVVDERPYEL RCSDRTSAWI
YDFGLRLPRH DGDGLADDAR ERFQNAFAAV WTGQAENDNF NELVLGAGLT WRQAMVLRAY
AKYLRQAGST FSQSYMEDTL RTNVHTTRLL VSLFEARMSP ERQRAGTELT DALLEELDAA
LDQVASLDED RILRSFLTLI KATLRTNHFQ KNEDGQPHAY LSMKLDPQAI PDLPAPRPAY
EIWVYSPRVE GVHLRFGKVA RGGLRWSDRR EDFRTEILGL VKAQMVKNTV IVPVGAKGGF
VGKRLPDPAV DRDAWLAEGI ASYKTFISGL LDITDNNVGG QVQPPKDVVR HDGDDTYLVV
AADKGTATFS DIANEVAQAY GFWLGDAFAS GGSAGYDHKG MGITARGAWE SVKRHFGELG
HDTQTEDFTV VGVGDMSGDV FGNGMLLSEH IRLVAAFDHR HIFLDPNPDS AVSYAERRRM
FELPRSSWAD YDTSLLSQGG GIHPRTAKAI PITPQVRKAL GIESRVAKMT PADLMKAILK
APVDLLWNGG IGTYVKAATE SHADVGDKAN DAIRVDGQDL RVKVVGEGGN LGLTQLGRIE
FALNGGRINT DAIDNSAGVD TSDHEVNIKI LLNELVREGD MTVKQRNKLL AEMTDEVGAL
VLRNNYAQNV ALANSVAQAP SLLHAHQRVM RRLGREGRLD RSLEFLPTDR QIRERLAAGR
GLTQPELAVL LAYIKITVAE ELITTDLPDD PYLQRLLHAY FPQALRQKFT EHVDGHALRR
EIVTTVLVND TVNTAGATFL HRMREETGAS TEEVVRAQTA ARAIFELGEV WDEVESLDNK
VPADVQTRMR LHSRRLVERG TRWLLGNRPQ PLELAETIEF FGERVAAVRS QLSKLLRGAD
VEWYQTIHDE LTAAGVPDDL ATRVAGFSSA FPTLDIVAIA DRLGKDPLSV AEVYYDLADR
LRISQLMDRI INLPRADRWQ SMARASIREE LYAAHAALTS DVLSVGDGGA SPEQRFKAWE
EKNASILQRA RTTLDEIQGS ETFDLANLSV AMRTMRTLLR TQR
//
