ID G0CH82_XANCA Unreviewed; 1645 AA.
AC G0CH82;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:AEL07518.1};
GN ORFNames=XCR_2645 {ECO:0000313|EMBL:AEL07518.1};
OS Xanthomonas campestris pv. raphani 756C.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL07518.1, ECO:0000313|Proteomes:UP000001633};
RN [1] {ECO:0000313|EMBL:AEL07518.1, ECO:0000313|Proteomes:UP000001633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=756C {ECO:0000313|EMBL:AEL07518.1,
RC ECO:0000313|Proteomes:UP000001633};
RX PubMed=21784931; DOI=10.1128/JB.05262-11;
RA Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA Leach J.E., White F.F., Salzberg S.L.;
RT "Two new complete genome sequences offer insight into host and tissue
RT specificity of plant pathogenic Xanthomonas spp.";
RL J. Bacteriol. 193:5450-5464(2011).
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DR EMBL; CP002789; AEL07518.1; -; Genomic_DNA.
DR KEGG; xcp:XCR_2645; -.
DR PATRIC; fig|990315.4.peg.2502; -.
DR HOGENOM; CLU_003404_1_1_6; -.
DR Proteomes; UP000001633; 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 33..164
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 398..487
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 561..622
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 764..1259
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1304..1638
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1645 AA; 183693 MW; 064F909EDB8DF725 CRC64;
MVATAPQEIT LEPVFAALRK RYPAARQSEV QLFAADFYRR MEEDEFPNHP PEQWAALAAD
MLEFARTRKA GTVNVRVFNP TLKSHGYESP HTLLQIVNDD MPFLVDSVSM TLSELGIGVH
VLGHPVLRIT RDKGGKLTAV GEGKSESLMV LEIDRQPADE MPKVEAAIRK VLAEVRAIVH
DWAAMREKMV MLADDLATRR LPMDDISRHE AQEFLRWAAS DHFTFFGYRE YRVEKQDGQE
VLAPVEESGL GLMRGHDISP ARPVTSLAAH GLNTSAKLKD ALILTKTNAR SRVHRVGYMD
YIGILEFDAK GRIVGEQRFL GLFTSSAYNR RPWEIPLVRQ RYEYVMSKSG LTPSSHSGKA
LRHILETLPR EELFQSNQDE LYRTAIGILG LQERVRSRMF LRRDKYSRFI SALVYIPRER
FNTDVRLRIE ALLKDALHGE YIDSSVVLGE SPLAQLHLIV RAKSGEALEF DTTALEARLA
HVLRNWHDAL REALVARHGE AHGLRMAANF GRALPAGYIE DSSIESAVAD VEHLAALDGP
DDLHLSLQEV RRDSAVRLDT GDGLRLKLYR QLDDIPLSDA MPMMENMGLR VISERPYRLQ
VSDTPVYIQD FEVESTAGHI DASSADAAFG EAFERIWNGD AENDGFNRLI LAAGLHWRQV
ALLRGYCKYL LQTATPFSQA YVEATFTRYP LLARLLVELF EARFDPSTCG ETKAQILAGQ
ERLREQLSVL ADGDEATLKA LEPVLQARGS DRAAQQEATR AALLKLMDRV SSLDEDRILR
SFIDVIDATL RTNYYQTSKD GKHGHCISFK LDSSLVPDLP KPRPYREIFV YGPRVEGVHL
RFGAVARGGL RWSDRREDFR TEVLGLVKAQ MVKNTVIVPV GAKGGFYVKR SPVGGDRDAI
QAEGIACYKL FIQSLLDITD NIVGGKIVPP TQVVRHDQDD PYLVVAADKG TATFSDIANG
LALDHGFWMG DAFASGGSVG YDHKGMGITA RGAWESVKRH FRALGRDCQS QDFSVVGIGD
MSGDVFGNGM LLSRHIRLLA AFDHRHIFLD PNPDAAASFA ERERLFALPR SSWADYDAKL
ISAGGGIYPR TLKSIELSAP VREALGLDAS FKQLSPNELM NAILKAPVDL FWNGGIGTYV
KATSESHGDV GDRANNGLRV NGGELRCKVV GEGGNLGLTQ LGRIEAAQTG VLLNTDFIDN
SAGVDTSDHE VNIKILLNDV VQAKKLTYDA RNKLLASMTN EVADLVLWDN YRQNQAISLM
ERMSVKRLGS KQHFIRTLEL QGLLDRQIEY LPSDAELSAR KARGQGMTRP ELSVLLSYSK
LVAFQQLLES DIPEDPYLSK ELQRYFPQPL QKKYADAMER HRLKREIIAT AVTNTTINRM
GATFLMRMQE DTGRSIAEVA KAYTISRETL DARALWTQID ALDGKVPESV QIDALEVIWR
LQRSFVRWLL SRPGQMPGIT AAVERYHGPF NDIRVASGVL PDAQRPVYEA SVQEWQEKGL
TPELAQQLCE LRYLEPAFDI IELARTRKLK PVEVSKVHFR LGEALRLPWL FEQIDALEVN
GRWHAVARGV LRDELAAHQR TLAGQVLSMP GASAEDKVAN WLARDDSSLR FTLAMLSDVA
EQKTLDYPTV SVAVQRLGQL AAHGV
//
