ID   A0A0J8VBX9_9GAMM        Unreviewed;      1609 AA.
AC   A0A0J8VBX9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:PSW23493.1};
GN   ORFNames=C9I94_15330 {ECO:0000313|EMBL:PSW23493.1};
OS   Photobacterium swingsii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=680026 {ECO:0000313|EMBL:PSW23493.1, ECO:0000313|Proteomes:UP000240481};
RN   [1] {ECO:0000313|EMBL:PSW23493.1, ECO:0000313|Proteomes:UP000240481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24669 {ECO:0000313|EMBL:PSW23493.1,
RC   ECO:0000313|Proteomes:UP000240481};
RA   Butler K.;
RT   "Whole genome sequencing of Histamine producing bacteria.";
RL   Submitted (JAN-2018) 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:PSW23493.1}.
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DR   EMBL; PYLZ01000008; PSW23493.1; -; Genomic_DNA.
DR   RefSeq; WP_048898349.1; NZ_PYLZ01000008.1.
DR   STRING; 680026.AB733_08380; -.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000240481; 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}.
FT   DOMAIN          34..172
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          401..490
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          546..625
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          723..1217
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1262..1599
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1609 AA;  183016 MW;  DC2B98AB12CE37AA CRC64;
     MTAPDPIVPV LLEKVYGLIQ DKIETPQQSL VEVFAQRLLG QLADDDLLQR NESDLYGAVL
     SLWHHLLKTD PTTTSVRVYN PTLSRYGWQS THTVVEIVVP DSPFLVDSVR MTLNRLGITS
     HLMLNGPYYF KRNESGTIVE ACGTEGDFQT LFHIEVDRLT DKSEMETLKR ELEQMLVDVD
     LVVTDWQAMQ DKMQSIAKEL ETAPLPVDDS SRAEALELLD WVTRHNFTFM GYHNYDLKAV
     EGDYQLCPTE EAGLGLLSKP NKARCLMLSD LPESARFEAR KPEIMILTKS NGQSKIHRPA
     YIDYIGIKRF AEDGSVIGEH RFVGLYASTA YHQTATNIPL IRNKMARILE SSGYTEGSHS
     WKALNNLLET YPRDELFQAT EKEMLDVGCG VVQMQDRDLL RLFVRRDPFG RFFSCMVYVT
     KERYNTELRS KTQAILKEYF GSEQNVEFTT FFSESPLART HYIVRVENNN FNIDVKAIEH
     NLVEAAASWE DRISDALVAN FGESRGTSLA KNYSRAFQRS YKEEMLPGSA VADIEQLESL
     SEENKLGMLF YRPQEEAADS RFVKLKLFHR DEPIHLSDVM PMLENLGLRV IGESPYQVTT
     SKGTVFWILD FAMLHNACTG IDLREARDRF QEAFSAIWHG TLESDGFNRL VLCAGLTGRE
     ITILRSYARY MRQVGFPFSQ HYIEETLSSH NDLARDLVAL FELRFDPKKK HSEKAEQTLI
     GKLNGKLDHV ESLDDDRIIR RYMEMILATQ RTNYYQLDEN GKNKPWLSLK LRPSDIPEIP
     QPVPFFEIFV YAPDIEGVHL RGGKVARGGL RWSDRQEDFR TEILGLVKAQ QVKNTVIVPV
     GAKGGFICKR QPQMTTREEI WAEGQRCYKR FIRALLDVTD NIIDGDLIPP ANVVRHDEDD
     PYLVVAADKG TATFSDLANS VSEDYNFWLG DAFASGGSNG YDHKKMGITA KGAWESVKRH
     FRELGTDCQT TDFTCAGVGD MAGDVFGNGM LLSKHIRLVA AFNHMHIFID PNPDSAKTWP
     ERERLFNLPR SSWEDYDQSL ISEGGGIFSR RSKSIKLTPQ IQKLLGTRKQ TMPPNELIRL
     ILQMEVDLLW NGGIGTYVKA ESETHTDVGD RANDALRING NELRAKVVGE GGNLGMTQLG
     RVEFAKRGGL VNTDFIDNVG GVDCSDNEVN IKILLNSLVA GGDLTYKQRN QLLESMEDEV
     GEIVLDDAYC QSESISVTQQ QQVQLLKEQI RFIHHLEREG KLDRALENLP DDETLAEREK
     SGMGLTRPEL AVLVAYGKMV LKEQLVTDEI SNDPYHARLL PAYFPAQLKE KYRAQMDNHP
     LRKELIATSL ANQMSNEMGC NFVTRLQEET GATVAEVSSA YAVGRSVFNF DKFFDQIREL
     DNVVSAETQY DMLYRCRRML RRATRWILRN RDRKLGIEQQ ISFYQPVVNT LNENLESYLV
     TEEVQEHKDQ AAVMVAQGVP QALAENIARL SSLYSAMDIA QIAKELKQEI DQISRVYFVV
     GAELSLHWFL QQVNNQSVDN HWQALARASF REDLDWQQRQ LTSAVITTMA DDATAEQGIE
     AWMQEHDKAI LRWESVLAEF KVGNVHEFAK FSVALRELML LNLNCRSSI
//