ID J2GSF6_9CAUL Unreviewed; 1616 AA.
AC J2GSF6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:EJL25758.1};
GN ORFNames=PMI01_04235 {ECO:0000313|EMBL:EJL25758.1};
OS Caulobacter sp. AP07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1144304 {ECO:0000313|EMBL:EJL25758.1, ECO:0000313|Proteomes:UP000007300};
RN [1] {ECO:0000313|EMBL:EJL25758.1, ECO:0000313|Proteomes:UP000007300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP07 {ECO:0000313|EMBL:EJL25758.1,
RC ECO:0000313|Proteomes:UP000007300};
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:EJL25758.1}.
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DR EMBL; AKKF01000228; EJL25758.1; -; Genomic_DNA.
DR RefSeq; WP_007673467.1; NZ_AKKF01000228.1.
DR PATRIC; fig|1144304.3.peg.4066; -.
DR Proteomes; UP000007300; 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 38..133
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 395..484
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 543..622
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 726..1221
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1266..1610
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1616 AA; 175893 MW; D9071162755179CE CRC64;
MVGEKLDPKA AAAQSEGLIS AFSAALGQGA LTEPLRQFAA QAQEDWSAEE LPGFAADDIA
HGLIDFWRFG ETASEPVSLR IRRARRADGT DLKSDLLEIV QPDRPFLVDS IMGAIAEQGF
SVRAMFHPVV ETATGRRSMI QVYLAPVGED REAALIAAVR ETLADVQLAV DDFDGMKALM
RRTIDALRDS PVAIPEVERA EGLAFLDWLE GDHFVFLGAR VYEYPRTADG GYAAEEPLYQ
PEGSLGVLRD QTRTVLRRES EPAILSPQVR DHLLLGAPLV VAKSNLRSKV HRRGYMDYVG
VRRYGADGKA SGEVRFVGLF TAEAYETPAH EVPVIRRKVE HVLDQAGKDP DSHNGKRLRN
ILETWPRDEL FQIPEGELLT MALGVLHLYD RPRVRLFARR DPFDRFISVL MFVPRERYDS
GVRERAGRIL AQAFEGRVSA YYPSFSDAPL ARVHYVLGVT PGKHGNPDLA DLEAAVAETA
RTWEDRFEVA VREGGAPGRV AETLARYLTA FPPGYRDQYD AAEALADIAV IDDLAEGEAV
RVRGFRHADD DKLTFRFKLY RPGAAAPLAD VLPILEHMGL KALIEDGFKL TPAAHTSVGG
VHGKVWVHEF TLRDEQGEHL SFGDVKSAFE AAFVAIWTGR AESDGFNRLV LELGVGWREA
ALIRALARYR QQTGLDPSQG VQEQALSDNP GVTRLILDLF RIKFDPAVRA DLKAREEQAK
AVEAKIGEAL QAVESLDADR VLRRIAALVG AIQRTNFFQV GEDGEPKPYI SYKIASRELD
DLPAPKPYRE IYVSAPHVEG VHLRFGPVAR GGLRWSDRRD DFRTEVLGLV KAQQVKNAVI
VPVGSKGGFF PKNLPRGGTP DAIRAEAIRA YKTFLSGLLD ITDNIDADNR VVPPVGVISH
DGEDPYLVVA ADKGTATFSD IANGVAEDYG FWLGDAFASG GSVGYDHKVM GITARGAWEA
VKRHFRELGK DIQAEPFTVV GVGDMSGDVF GNGMLLSKQT RLLAAFDHRH IFLDPDPDVA
VSWAERDRMF KLPRSSWEDY DKSLISQGGG VFPRTLKQIP LSPEVRAMLE IKAETVAPNE
LLTAILKAKA ELLYFGGIGA YVKARGESQA EAGDKANDAI RVNGADLRVK VVGEGANLGL
TQAGRIEFAQ LGGHINTDAI DNSAGVDSSD HEVNIKILTG ILERGGKLTR DSRNQLLPTM
TDDVASHVLA DNYDQTLALT LMESDAVSEV DSHARFMAEL EAKGRLDRRV EGLPEAAVLS
ERAKAGKGLT RPELAVLLAY GKIDLFDDIV ASEAPDDPWF EATLLGYFPP ALGKYADEMQ
RHRLKREIIA TVLDNQMINM CGPTFPSRLR AAAGCDTTAL VTAFAAARQI LGIDALWDQV
SALDGKASAA GQTALYKALA YALRSLTFWL ARRAFRDKLA VAKLVEAYGP SVKALSALTP
AILSSFEQKA SAKRAKVYMA DGAPEALAQA VAALQPLTTA ADLVDLGNAS SWPVENVARL
YHQVGAAFGF DRLRGAAGSF VGGDPFERLA VRRLIEDMLG EQTAITQAVL KFSANAQAGD
DEASAKAATT SWAALRTDTV RAAKRTVEDI EQAGGGWTFA KLTIANAALR GLASAS
//
