ID A0A171BTX8_9ACTN Unreviewed; 1642 AA.
AC A0A171BTX8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:GAT84903.1};
GN ORFNames=STXM2123_5604 {ECO:0000313|EMBL:GAT84903.1};
OS Streptomyces sp. F-3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT84903.1, ECO:0000313|Proteomes:UP000078145};
RN [1] {ECO:0000313|EMBL:GAT84903.1, ECO:0000313|Proteomes:UP000078145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.;
RT "Streptomyces sp. F-3 geneom sequencing.";
RL Submitted (MAY-2016) 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:GAT84903.1}.
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DR EMBL; BDDR01000058; GAT84903.1; -; Genomic_DNA.
DR RefSeq; WP_067399569.1; NZ_BDDR01000058.1.
DR STRING; 1840095.STXM2123_5604; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000078145; 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:UP000078145}.
FT DOMAIN 47..194
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 579..648
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 755..1253
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1298..1635
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
FT REGION 18..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1642 AA; 184144 MW; 870639DB39F103C0 CRC64;
MQTKLDEAKA ELLERAARVA ENSPTGGHLP VGRTGEGAPD RDSVLAFLQR FYLHTAPEDL
MDRDPVDVFG AAHSHYRLAE NRPQGTANVR VHTPTVEENG WTCSHSVVEV VTDDMPFLVD
SVTNELTRQG RGIHIVIHPQ FVVRRDVTGK LIEVLPDASP GEPLPQDALV ESWIHVEIDR
ETDRDDLKRI TTELLRVLSD VREAVEDWGK MREAAIRLAE GLSEESLPDD LRPQEIEEAR
ELLRWLADDH FTFLGYREYQ LRDDDSLAPL PGTGLGILRA DSPHTGDDGR PVSPSFERLP
PDVRAKAREH KLLVLTKANS RATVHRPSYL DYIGVKKFDD KGEVVGERRF LGLFSSAAYT
ESVRRIPVIR RKVDEVLERS GLSPNSHDGR DLLQILETYP RDELFQIPVG ELQSITTSVL
HLQERRRLRL YLRKDEYGRY YSALVYLPRD RYTTAVRLRI IDILKEELGG TSVDFTAWNT
ESVLSRLHFV VRVPRGTQLP QLSDSDRERI EARLAEAARS WEDAFSEALV VELGEERAAE
LLRHYAGAFP EGYKADHTPR AAVADLVNLD QLDEDRTFVL SLYEPVGAAP DERRFKMYQK
GGLVSLSAVL PVLSRLGVEV IDERPYELRC ADRTTAWIYD FGLRMPREVS GEFLGDDTRE
RFQDAFAAVW TGKAENDGFN ALVLSAGLTW RQAMMLRAYA KYLRQAGSTF SQDYMEDTLR
HNVHTTRLLV SLFEARMSPD RQSAGSELVD ALLEEIDAAL DQVASLDQDR ILRSYLTLIK
ATLRTNFFQK DKDGRPHDYV CMKFDPQAIP DLPAPRPAYE IWVYSPRVEG VHLRYGKVAR
GGLRWSDRRE DFRTEILGLV KAQMVKNTVI VPVGAKGGFV AKQLPDPNVD RDAWMAEGIA
SYKTFISALL DITDNMVAGE VVPPKDVVRH DGDDTYLVVA ADKGTARFSD IANEVAQSYD
FWLGDAFASG GSAGYDHKGM GITARGAWES VKRHFRELGV DTQTQDFTVV GIGDMSGDVF
GNGMLQSEHI RLVAAFDHRH IFVDPNPDAA VSYAERRRLF ELPRSSWADY NTELLSAGGG
VFPRTAKSIP VNAHMREALG IEDGVTKMTP AELMQAILKA PVDLLWNGGI GTYVKASTES
HADVGDKSND AIRVDGRDLR VRVVGEGGNL GFTQLGRIEF AMHGGRINTD AIDNSAGVDC
SDHEVNIKIL LNGLVADGDM TVKQRNKLLA EMTDEVASLV LRNNYAQNTA IANALAQSKD
MIHAQQRFMK HLVREGHLDR ALEFLPTDRQ IRERLSAGRG LTGPETAVLL AYTKITVAEE
LLRTSLPDDP YLRSLLHAYF PTPLRERFAD RIDNHPLRRE ITTTVLVNDT VNTGGTTYLH
RLREETGASL EEIVRAQTVA RAIFRSAQVW DAVEALDNKV PADVQTRIRL HSRRLVERGT
RWLLNNRPQP LELGETVEFF SDRVGQVWAA LPKLLKGADL EWYQQVYDEL SGAGVPDELA
TRVAGFSSVF PALDIVSVAD RMGKDAMDVA EVYYDLADRL DITRLMDRVI ELPRTDRWQS
MARAAIREDL YATHAALTAD VLAVGNGSST PEQRFKVWEQ KNAAILARAR ATLEEIHTSE
TFDLANLSVA MRTMRTLLRT HS
//
