ID J2XS87_9PSED Unreviewed; 1629 AA.
AC J2XS87;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:EJN34072.1};
GN ORFNames=PMI35_00600 {ECO:0000313|EMBL:EJN34072.1};
OS Pseudomonas sp. GM78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144337 {ECO:0000313|EMBL:EJN34072.1, ECO:0000313|Proteomes:UP000007302};
RN [1] {ECO:0000313|EMBL:EJN34072.1, ECO:0000313|Proteomes:UP000007302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM78 {ECO:0000313|EMBL:EJN34072.1,
RC ECO:0000313|Proteomes:UP000007302};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJN34072.1}.
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DR EMBL; AKJF01000021; EJN34072.1; -; Genomic_DNA.
DR RefSeq; WP_008055135.1; NZ_AKJF01000021.1.
DR PATRIC; fig|1144337.3.peg.590; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000007302; 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 35..178
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 407..496
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 552..630
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 1629 AA; 182888 MW; 7825102EBE9864D7 CRC64;
MAFFTAASKA DFQHQLQAAL AQHISEQALP QVALFAEQFF GIISLDELTQ RRLSDLAGCT
LSAWRLLERF DHAQPQVRVY NPDYERHGWQ STHTAVEVLH HDLPFLVDSV RTELNRRGYS
IHTLQTTVLS VRRGSKGELL EILPKGTQGD DVLQESLMYL EIDRCANTAE LNVLTRELEQ
VLGEVRVAVS DFEPMKAKVQ EILTHLDNSQ FAIDADEKSE IKGFLEWLVG NHFTFLGYEE
FVVSDEADGG HIVYDKDSFL GLTKLLRAGL TYDDLRIEDY AVNYLREPTL LSFAKAAHPS
RVHRPAYPDY VSIREIDANG KVIKECRFMG LYTSSVYGES VRVIPYIRRK VAEIERRSGF
QAKAHLGKEL AQVLEVLPRD DLFQTPVDEL FSTVMSIVQI QERNKIRVFL RKDPYGRFCY
CLAYVPRDIY STEVRQKIQQ VLMDRLKASD CEFWTFFSES VLARVQLILR VDPKNRIDID
PQQLENEVIQ ACRSWQDDYS ALTVETFGEA HGTNVLADFP KGFPAGYRER FAAHSAVVDM
QHLLNLNEKN PLVMSFYQPL GQVGQRELHC KLYHADTPLA LSDVLPILEN LGLRVLGEFP
YRLRHNSGRE FWIHDFAFTA AEGLDLDIQQ LNDTLQDAFV HIVRGDAEND AFNRLVLTAG
LPWRDVALLR AYARYLKQIR LGFDLGYIAS TLNNHTDIAR ELTRLFKTRF YLARKLSSDD
LEQRLEHAIL TALDDVQVLN EDRILRRYLD LIKATLRTNF YQTDANGHNK SYFSFKFNPH
LIPELPKPVP KFEIFVYSPR VEGVHLRFGN VARGGLRWSD REEDFRTEVL GLVKAQQVKN
SVIVPVGAKG GFLPRRLPLG GSRDEIAAEG IACYRIFISG LLDITDNLKD GALVPPANVV
RHDDDDPYLV VAADKGTATF SDIANGIAID YGFWLGDAFA SGGSAGYDHK KMGITAKGAW
VGVQRHFRER GINVQEDSIT VVGVGDMAGD VFGNGLLMSD KLQLVAAFNH LHIFIDPNPN
PATSFAERQR LFDLPRSAWS DYDTSIMSEG GGIFSRSAKS IAISPQMQER FDIQADKLTP
TELLNALLKA PVDLLWNGGI GTYVKASSES HADVGDKAND ALRVNGNELR CKVVGEGGNL
GMTQLGRVEF GLNGGGSNTD FIDNAGGVDC SDHEVNIKIL LNEVVQAGDM TDKQRNQLLA
SMTDEVGGLV LGNNYKQTQA LSLAARRALP RIAEYKRLMN DLEGRGKLDR AIEFLPAEDQ
LNERVAAGHG LTRAELSVLI SYSKIDLKEQ LLGSLVPDDD YLTRDMETAF PPTLVNKFSE
AMRRHRLKRE IVSTQIANDL VNHMGITFVQ RLKESTGMSP ANVAGAYVIV RDIFHLPHWF
RQIENLDYKV SADVQLELMD ELMRLGRRAT RWFLRARRNE QNAARDVAHF GPHLAALGLK
LDELLSGEIR ETWQTRYQAY VAAGVPELLA RMVAGTTHLY TLLPIIEASD VTGQDPADVA
KAYFAVGSAL DITWYLQQIS ALPVENNWQA LAREAFRDDV DWQQRAITIS VLQEGNGTQD
VETRLASWMA QHESMIGRWR AMLVEIRAAS GTDYAMYAVA NRELLDLALS GQAVVPVTAN
ASAELEPAA
//
