ID A0A0B5EUK7_STRA4 Unreviewed; 1645 AA.
AC A0A0B5EUK7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:AJE82915.1};
GN ORFNames=SLNWT_2539 {ECO:0000313|EMBL:AJE82915.1};
OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS NBRC 107858).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE82915.1, ECO:0000313|Proteomes:UP000031523};
RN [1] {ECO:0000313|EMBL:AJE82915.1, ECO:0000313|Proteomes:UP000031523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC {ECO:0000313|Proteomes:UP000031523};
RA Lu C.;
RT "Enhanced salinomycin production by adjusting the supply of polyketide
RT extender units in Streptomyce albus DSM 41398.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP010519; AJE82915.1; -; Genomic_DNA.
DR STRING; 1888.Salbus254_2141; -.
DR KEGG; sals:SLNWT_2539; -.
DR Proteomes; UP000031523; 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 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:UP000031523}.
FT DOMAIN 46..195
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 429..522
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 578..649
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 759..1256
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1301..1638
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1645 AA; 183153 MW; D32758A8B3F97ED1 CRC64;
MQTKLDEAKA ELLERAARVA ENSPVGGILP TEAQGAKSDQ AAVLAFLQRY YLHTAAEDFV
GRDPDDVFGA AFSHLRLAEN RPQGTANVRV HTPTVEENGW TCSHSVVEVV TDDMPFLVDS
VTNELTRQHR GIHVVIHPQI VVRRDVTGRL LEVLTSATAG DRGSLPHDAL IESWIHVETD
RETDRSDLKQ ITADLLRVLS DAREAVEDWE KMREAALRIA EELPGEPTAD DLPAQEVEEA
RELLRWLAAD HFTFLGYREY ELREDDSLAA VPGTGLGILR ADPHHSGEEH PVSPSFSRLP
ADARAKAREH KLLVLTKANS RSTVHRPSYL DYVGVKKFDA EGNVIGERRF LGLFSSAAYT
ESVRRVPVIR RKVEEVLRGA GFSPNSHDGR DLLQILETYP RDELFQTPPD ELRAIVTSVL
YLQERRRLRL YLRKDEYGRY YSALVYLPRD RYTTGVRLRI IDILKEELGG TSVDFTAWNT
ESVLSRLHFV IRVPTGTELP QLSDADKDRI EARLVEAARS WQDAFTEALY AELGEERAAE
LARRYAGAFP EGYKADHSPR SGVADLVHLE AIQSGAKDFA LSLYEPVGAQ PGERRFKIYR
AGGQVSLSAV LPVLQRLGVE VTDERPYELR CADRPNAWIY DFGLRMPKAP GPSGDYLGDD
GRDRFQEAFE ATWKGHAEND GFNSLVLRAG LSWRQAMVLR AYAKYLRQAG STFSQDYMED
TLQNNVHTTR LLVSLFEARM SPDHQRAGTE LTDGLLEELD GALDQVASLD EDRILRSFLT
VIKATLRTNF FQETEGGSPH DYVSMKFDPQ AIPDLPAPRP AYEIWVYSPR VEGVHLRFGK
VARGGLRWSD RREDFRTEIL GLVKAQMVKN TVIVPVGAKG GFVAKQLPDP SEDRDAWLAE
GIACYRTFIS ALLDITDNLV AGEVVPPADV VRHDEDDTYL VVAADKGTAT FSDIANEVAE
SYEFWLGDAF ASGGSAGYDH KGMGITARGA WESVKRHFRE LGHDTQTEDF TAVGVGDMSG
DVFGNGMLLS EHIRLVAAFD HRHIFIDPKP DAAVSYAERR RLFELPRSSW ADYNTELLSA
GGGIFPRSAK AIQLNSHVRE ALGIEKGVAK MTPADLMRAI LQAPVDLLWN GGIGTYVKSS
QESNADVGDK ANDAIRVDGA DLRAKVVGEG GNLGLTQLGR IEFALGGGRI NTDAIDNSAG
VDTSDHEVNI KILLNAVVGE GDMTVKQRNK LLAEMTDEVG RLVLRNNYAQ NTALANAEAQ
SPSLLHAHQR FMRRLERDGH LDRDLEFLPT DRQIKERLAG GRGLSQPELS VLLAYTKITA
ADELIRTTLP DDPYLRGLLL AYFPAALRER FPEQIDGHAL HREIVTTVLV NDTVNTGGST
FLHRLREESG ASLEEIVRAQ LAARTIFGMS EVWDAVEGLD NIVDADVLTR IRLHSRRLVE
RGTRWLLNNR PQPLQLQETV DFFAEGVAAV WDELPKLLRG ADQEWYQRIR EELTEVGVPD
ELAQRVAGFS AAFPTLDIVA IADRMGKEPL AVAEVYYDLG DRLRISQLMD RIIELPRTDR
WQSMARASIR EDLYAAHAAL TADVLAVGNG GSSPEQRFKA WEEKNAAILG RARTTLDEIQ
SSDAFDLANL SVAMRTMRTL LRTHS
//
