ID C5BKZ4_TERTT Unreviewed; 1607 AA.
AC C5BKZ4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Putative NAD-glutamate dehydrogenase {ECO:0000313|EMBL:ACR12832.1};
GN OrderedLocusNames=TERTU_2429 {ECO:0000313|EMBL:ACR12832.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR12832.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR12832.1, ECO:0000313|Proteomes:UP000009080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
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DR EMBL; CP001614; ACR12832.1; -; Genomic_DNA.
DR RefSeq; WP_015818944.1; NC_012997.1.
DR STRING; 377629.TERTU_2429; -.
DR KEGG; ttu:TERTU_2429; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_6; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000009080; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009080}.
FT DOMAIN 37..179
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 404..493
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 548..618
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 727..1216
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1261..1597
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1607 AA; 181320 MW; 910C9D64E6A2C358 CRC64;
MEISQPHVND REHFLTVFDK WVEQNKQKET DPGFLKFAQV YLARFPLEDW VGRQIGDLFG
LCYGLFMTLK NSARKPVVEV YNPSLSEHGW QSGRTIVVIL QRDMPFLVDS IRVLFNKKEI
PIYIIKSRVL NVKRGGEFSV EQGGAKPSKE KNISREALIY LEISLHPASD ELVRIKRELQ
KVLADVSAVV DDHDSILARL DEAQGSISQM GESTAEIVAF LSWLRHRHFV FLGFRDYNLI
DQADGRVLEE NADARMGVFR GIKAENTRVP EAQFSDGIRN FYEGSDIVCF SKAATHSSVH
RAVYPDYVVV KKLDAQGNAL GEVRFLGLFT YEVFSQSPFD IPILRLKVNS IVENSGLDPN
SHDGKNLFRT IENYPRTELM LTDTATLENN ILAIANLNER HLVKLIARAD PFGNFVTCNV
FVPRDVYTSA SRQRIQDILG EALGSNDFDF NTFFSESNLV RAQFVFRIDP SVKRELNLAE
LEDSIAEVTR NWTDHLRSSL YEEYGEAKGT AYFNAFKNGF TPSYQEYFDA RFAVQDIKLI
EELKNEQDIA MNFYRPFGAD ETAIRFRILH LNEPLVLSDV IPLLENLGLR VIGEHPYQIF
QKNGKGVWLH DFQLVLGLPV NPDISSAKLL FEDAFEAIWR GQAESDPFNK LVLAARLNWR
EVCVLRAYAG YMKQVGFSSD QAFVADTLLR YLDITRDLVA IFKSRFDPRL NRDNKSKERG
ERLKKKVLDA LDAVPNLNED LVLRHYLQLI DGTLRTNYFR ANRDYISFKF SPRTIPDIPE
PRPLFEIYVY SPRVEGVHLR GGKVARGGLR WSDRLQDYRT EVLGLVKAQQ VKNAVIVPTG
AKGGFVSKNP PKTGGRKAVL DEGIACYKTF IRGLLDLTDN FVAGEVIPPP EVIRHDEDDP
YLVVAADKGT ATFSDIANAI SIEYSHWLGD AFASGGSQGY DHKGMGITAR GAWVSVQRHF
REKGIDIQKE DFSVIGIGDM AGDVFGNGML LSEHICLTAA FNHMHIFIDP TPNAAATFTE
RQRLFQTPGI TWEDFDKSLI SAGGGVFSRA DKYIAISPQM REVFAITADK LTPTQLINAL
LKAPVDLIWN GGIGTYVKAS IETHTDVGDK ANDAVRVNGL ELRCQVFGEG GNLGMTQLGR
VEYALSGGAC NTDFIDNAAG VDCSDHEVNI KILLDEMVAA GDLTAKQRNA LLVEMTDDVA
ELVLQNNYRQ TQALSIAQFH AATRDNEYRR FITFLENRGR LDRSLEFIPT DDQIAERQAH
GKVLTRPELS VLISYAKVML KEELTDSDLA EDPYIARAIE SAFPQTIVHK FPEELYRHRL
KKEIVGTQLA NDLINNLGIT VGHRLLETTG ARSDQIARAY VVSRDVFEFE EFQDYIKSLD
NKVSAEFQAE LTSNMIRRVR RGTRWFLRNR RQDLSPEADV AFFKESLDAV YAASAEAIEG
SAREEWLARS KRFEELALPG VWALRLAMPD NLFSGLGVVE SARMAGKDIR PVTDMFFDLL
DKLDLNWFAS QLSEIKVDTY WQAIARETYL DDLETALRRL TVAMVNAQDK SGAAGLFEQW
LGDNASLIVR WKQMITEVQA SPGTDYAMFA VALRELGDLV DVTEHWV
//
