ID E4PFW3_MARAH Unreviewed; 1628 AA.
AC E4PFW3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:ADP98033.1};
GN OrderedLocusNames=HP15_2269 {ECO:0000313|EMBL:ADP98033.1};
OS Marinobacter adhaerens (strain DSM 23420 / HP15).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP98033.1, ECO:0000313|Proteomes:UP000007077};
RN [1] {ECO:0000313|EMBL:ADP98033.1, ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX PubMed=21304739;
RA Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA Glockner F.O., Grossart H.P., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT diatom-interacting marine microorganism.";
RL Stand. Genomic Sci. 3:97-107(2010).
RN [2] {ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001978; ADP98033.1; -; Genomic_DNA.
DR RefSeq; WP_014577586.1; NC_017506.1.
DR STRING; 225937.HP15_2269; -.
DR KEGG; mad:HP15_2269; -.
DR PATRIC; fig|225937.3.peg.2290; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_6; -.
DR Proteomes; UP000007077; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 35..178
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 410..498
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 553..631
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 734..1227
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1272..1609
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1628 AA; 185703 MW; B447512A2FB0E327 CRC64;
MNALTVASKD QFFEQLADAF AKKISKTEAK KISEFAKQHY AHIPLEELVS RRFADTYGAV
LAAWQFLQKR SAEETPVAVF NPDLESDGWQ STHTVVFILH PNIPFLIDSL RIAINHREIG
THSIQHSILQ VNRDQNGKLE KLHTSKKKAS GSDYEAFIVL EIDRHSNPED LRDLEDTLQN
VLHEVRIAVS DFPVVTEKVN EILGELDNTT AGINEEQKEE ARAFLEWLAR DHFTFLGYDE
YDFAKDKSGM VVRRVENSEL GILRVNNERP DRVRLNELPQ RTRHEMTRSD DIFIFAKSAQ
RSRVHRPAYP DYIAVKKFNS KGEVVGERRF LGLYTARVYN ERPDEIPLLR RKFQSVMKRS
GFLRDDYAGK ELEQILTVYP RDELFQIEQD ELLKVAKSIL YIQERRRIEL FLREDVYGQF
VTCLAFFPRD IYNTELRLKV EQVLVDRLGA EDVEFVTHFS ESVLARVQFT IRVPQVENRQ
LPTAEIREKV IELAQSWRDG LSEALSEAWG EEQGNELYRL WAGGFPASYT DMFSPRRAAI
DLEHIASSAN NHDLAMSFYR ALEEDESTLH FKLFYPDEPL PLSDVMPIFD NLGFRVIGEH
PFEVIDRHNK TVWIHDFTLQ AHQGTVVDIH RIRPIFEELF RRVWYGEAEN DAFNRMLLSS
YMSWREIALL RTYARYMRQI RFSNSQTFIS NTLVNHVELT RLLLEFFEIR FNPERYQSPG
KSQAAQQKLE IEFNAGLENV ENLSEDRVLR LYLELIQATL RTNYYQHGES GGPKPYISVK
FDPSRIPDMP LPMPMFEIFV YSPRVEGVHL RGGKVARGGL RWSDRFEDYR TEILGLVKAQ
QVKNAVIVPV GAKGGFVAKR LPDPSDREAF QAEGIEAYKT FIRGLLDITD NLVDAGIAPP
ERVIRHDDDD HYLVVAADKG TATFSDIANG LAAEYGFWMG DAFASGGSNG YDHKKMGITA
RGAWVSVERH FREMGINPGL DEFTAIGIGD MGGDVFGNGM LCSEKTKLVA AFNHVHIFVD
PSPDPEKSYK ERMRLFGLPR SAWTDYDSKL ISKGGGVFSR NSKSIPVSPE MKKLLGIKSD
RVPPNMLISH ILKAQVDLLW VGGIGTYVKA ASESHSDVGD KANDGLRING SDLRCKVVGE
GGNLGLTQLG RIEFALKGGR LNTDFIDNSG GVDCSDHEVN MKILLNRAVA MGDLTNKQRN
IMLEEMTDDV AELVLKNNYR QTQAISIASE DAATRLEEYR RLMNTFESEG KLNRALEFLP
DDETLSERKL DKKGLTRPEL SVLISYVKGD LKQTLIDSTL PDDPLLAGEM YKVFPRDLTQ
KFSKELGEHQ LRREIIATQI ANDMVNHMGI TFVERLNQST GADAASIALA WIIARDVFRI
DNWWDRIEAL DFHVSAQLQM ELMQDLMRLM RRSVRWLLRN RRAELSIQHH MERFADSVWA
ITAGLPEYLG DQAKTTWEKR HQALVDAGLP SELASVVSGT GHLYSSLGII EAHEASGMPL
KTVANLYYEL GDRLDLNWFA SAIASLQPGS HWQALARESF REDLDWQQRA LTTGVLKLAD
KPEDVPACVE AWLSRHQQMI DRWKSMLSEL KGVREPEYAM FSVALRELLD LAQSTMHQPH
AEVEVQTN
//
