ID Q5GZ15_XANOR Unreviewed; 1753 AA.
AC Q5GZ15;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:AAW76056.1};
GN OrderedLocusNames=XOO2802 {ECO:0000313|EMBL:AAW76056.1};
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331 {ECO:0000313|EMBL:AAW76056.1, ECO:0000313|Proteomes:UP000006735};
RN [1] {ECO:0000313|EMBL:AAW76056.1, ECO:0000313|Proteomes:UP000006735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85 {ECO:0000313|Proteomes:UP000006735};
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.M., Park Y.J., Park D.S., Kang H.W., Kim J.G., Song E.S., Park I.C.,
RA Yoon U.H., Hahn J.H., Koo B.S., Lee G.B., Kim H., Park H.S., Yoon K.O.,
RA Kim J.H., Jung C.H., Koh N.H., Seo J.S., Go S.J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
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DR EMBL; AE013598; AAW76056.1; -; Genomic_DNA.
DR STRING; 291331.XOO2802; -.
DR KEGG; xoo:XOO2802; -.
DR HOGENOM; CLU_003404_1_1_6; -.
DR Proteomes; UP000006735; 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 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:UP000006735}.
FT DOMAIN 136..269
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 501..590
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 664..724
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 867..1367
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1412..1746
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1753 AA; 195390 MW; 579C4A438CF1DFDD CRC64;
MTVAVSCVQW LMCQARDRTL PVVAIRRRSR AAVFHELHRC SAFARCHGPW RAAYLLYAAR
RRHRAPVQFI FQPSIPALLM TANKAASKSS TTSVKPAAER AVPVLATEPQ AVTLAPVFAA
LRKRYPAARQ AEVQAFAADL YRRMEEDEFP NHPPEQWAAL ASDMLEFTRV RKAGMVNVRV
FNPTLKSHGY ESPHTLLQIV NDDMPFLVDS VSMTLADLGI GVHVQGHPVL RIARDKGGKL
TAVGEGKSES LMVLEIDRQP PEEMPKLEAA VRKVLAEVRA IVHDWAAMRE KMVMLADDLA
TRRLPIDDIS RHEAQELLRW AAADHFTFFG YREYRVEKQD GQDVLAPLED TGLGLMRGHD
TSPARPVTTL AAHGLNASSK LKDALILTKT NARSRVHRVG YMDYIGILEF DAKGRIVGEQ
RFLGLFTSSA YNCRPWEIPL VRQRHEYVMS KSGLAPSSHS GKALRHILET LPREELFQSN
EEELYRTAIG ILGLQERVRS RMFLRRDKYS RFISALVYIP RERFNTDVRL RIEGLLKDAL
HGEYIDSSVV LGESPLAQLH LIVRPKSGEA LEFDTTELES RLAHLLRNWR DALREALVAR
HGEANGLRMA ANFGRALPAG YIEDSSIESA VSDVEHLASL GGPDDLHLSL QEIRRDDGVR
LDAGRGLRLK LYRQLDDIPL SDAMPMMENM GLRVISERPY RLQVGETPVY IQDFEVESTA
GEINAAHADA SFGEAFKRIW NGDAENDGFN RLILAAGLHW RQVALLRGYC KYLLQTAVPF
SQAYVEATFT RYPLLARLLV ELFEARFDPS TGSETKAQIF AGQERLREEL SALAGGDDAT
LKALDTVLEA RGGDRDAQHE ATRATLLKLM DRVSSLDEDR ILRSFMDVID ATLRTNYYQA
DKNGKHPHCI SFKLDSARVP DLPKPRPYRE IFVYGPRVEG VHLRFGAVAR GGLRWSDRRE
DFRTEVLGLV KAQMVKNTVI VPVGAKGGFY VKRSPVGGGS TTENRDAIQA EGIACYKLFI
QGLLDITDNI VGGKIVPPPQ VVRHDHDDPY LVVAADKGTA TFSDIANGLA LDHGFWLGDA
FASGGSVGYD HKGMGITARG AWESVKRHFR AMGRDCQSQD FSVVGIGDMS GDVFGNGMLL
SKHIRLLAAF DHRHIFLDPN PDAAVSFAER DRLFKLPRSS WADYDAKLIS AGGGIYPRTL
KSIDISAPVR EALGLDANVK QLSPNALMNA ILKAPVDLFW NGGIGTYVKA ASESHTDVGD
RANNGLRVNG GELRCKVVGE GGNLGLTQLG RIEAAQTGVL LNTDFIDNSA GVDTSDHEVN
IKILLNDMVQ AKKLTYDARN TLLASMTDEV AELVLWDNYR QNQAISLMER MSVKRLGSKQ
HFIRTLELQG LLDRQIEFLP SDAELSARKA RGQGLTRPEL SVLLSYSKLV AFQQLLESDI
PEDPYLSKEL QRYFPQPLQK KYADAMERHR LKREIIATAV TNATINRMGA TFLMRMQEDT
GRSIGEVAKA YTISRETLDA RALWTQIDAL DGTVSEAVQI DALEVIWRLQ RSFVRWLLLR
PGQMPGITAA VERYHGPFND IRVASGVLSH AQRPQYEASV QEWQDKGLTP ALAQQLSELR
YLEPAFDIIE TARTRKLKPV DVSKVHFRLG EALRLPWLFE QIDALEVNGR WHAVARGVLR
DELAAHQRAL VGQALTMPGS SAEDKVANWL ARDDSSLRFT LAMLIDVAEQ KTLDYPTVSV
AVQRLGQLAA HGV
//
