ID A0A165U2G0_9GAMM Unreviewed; 1627 AA.
AC A0A165U2G0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:KZX58779.1};
GN ORFNames=A3709_17430 {ECO:0000313|EMBL:KZX58779.1};
OS Halioglobus sp. HI00S01.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Halioglobus.
OX NCBI_TaxID=1822214 {ECO:0000313|EMBL:KZX58779.1, ECO:0000313|Proteomes:UP000077184};
RN [1] {ECO:0000313|EMBL:KZX58779.1, ECO:0000313|Proteomes:UP000077184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI00S01 {ECO:0000313|EMBL:KZX58779.1,
RC ECO:0000313|Proteomes:UP000077184};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-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:KZX58779.1}.
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DR EMBL; LWEE01000030; KZX58779.1; -; Genomic_DNA.
DR RefSeq; WP_066052240.1; NZ_LWEE01000030.1.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000077184; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077184}.
FT DOMAIN 36..177
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 405..494
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 550..627
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 729..1223
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1268..1605
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1627 AA; 184358 MW; AA92BC8048077AF2 CRC64;
MTWENHKKAL LDSLERRIDD RAESADKASL KHLSSALLRR LSAEDLHGTA VENLYGCTYQ
LLEIFRHWDG EVPKVEFFNP QLHRDGWEST STILAILCPG IPFVTASVRG ELNRRNLPIH
IVASTNVVVE RDANGELQEI LGYMPETPEG ASSEAIIYFE LGRRSDPSDM SELRQTLLDI
LGEVMEVVTD FPAMNDQLES VVEDISCSDC VEAPYRDEAT AFLVWLREQH MTMLGYEYLE
VTYKGSTPNI SVAADRSLGL LRHRGTRGVA DLQADLASMS LDELQHRQLS FSKSRNRSRV
HRLTYPDYVE ARVFDEQGRV IGQHRFIGLY TSSVYTTHPK FIPILRRKVA AIMDMSHVDW
AEHETRELSR VLEMYPRDEL FQSNIADLNV VVNAINRIQE RRQTRLFVRR DAHGKFVSCI
VFVPRDRYTT ELREQIGEIL TRAYDAEESE FTTQFSESIL VRSHFVLRVD PANPIDCDPA
ELEEELVQAT LAWEDRLRNR LVEEFGEELG NAHANELGGG FPPGYRDDCD PRMAVADIRK
ILPLAAGKSL ELSLYRLAED SVTTLRLRLY HRGQSLPLSD VLPILENLGL RVTSERPYEI
RSRDGERFWV QEFTVHYSLS QDFDLDDIKE EFEDAFARIW FGEAESDSFN RLLIGTRLSW
REIAMLRAYA RYLRQLQFPF SVEYIAETMA SHLHITARIV EMFLTRFSPV FDGDEDWRAE
REMSVEQRIL EMLDEVQNLG QDRIIRQYLK VIKATLRTNF FQQEADGSLK PYMSFKLSPA
AIPDVPQPIP MFEIYVYSPR VEGVHLRGGR VARGGLRWSD RQEDFRTEVL GLVKAQQVKN
AVIVPVGAKG GFVARQLNGA MSREEVQEEG IACYRMFIRG LLDLTDNRGD IHVIRPPHVV
AKDEDDPYLV VAADKGTATF SDIANQISAD YDFWLGDAFA SGGSVGYDHK KMGITARGAW
VSVQRHFREM GVDVQSTDFT VVGVGDMAGD VFGNGMLLSE HIKLVAAFNH MHIFIDPNPD
PASSYAERKR LFGQPRSAWS DYDTTLISEG GGVFLRSAKS IAISAQMREL FDISDKQLTP
NELIGYLLRA PVDLLWNGGI GTYVKASSEA HVDVGDKAND GVRVNGDELR CRVVGEGGNL
GMTQLGRVEY GLSGGRSNTD FIDNAGGVDC SDHEVNIKIL LNAVVARGDL TEKQRNALLE
KMTDDVADLV LHNNYRQVQS ISLAEMQAGE RFEEYLRFME TMEEMGRLDR ALEFLPSAED
MLERRSRGQP LTRPELSVLI SYSKGVLKEE LIASDLGRDP YLANAVVTAF PAQLVDAYPE
DIRTHRLHRE IMCTQVANDI VNRMGLNFIL RLRKATGASI ADVARAFTTV MEVFNLRELW
DQIEAMDHEV SAEVQQDMML RLIRLVKRAS RWLLRNRRHD LAPTPLIAEF RPGLAELRET
FRDLLRGRVL EQYEEIAEHY LGEGVDETVA HRVAGNHLAY TALGIIQAAK ESGAPLTDVA
SLYYAMGDQL ELDWFGNQIL GAKVTNEWQA LARDTYLEDL EWQQRTLAVG ALHHLPEDRN
LLTCLSDWAK QEQVLLSRWQ EMLAELHATE VPDFAMFAVA NRELLDLAQS SVRAAMPDCG
NSPASEE
//
