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Database: UniProt
Entry: B6Y9H2_9RICK
LinkDB: B6Y9H2_9RICK
Original site: B6Y9H2_9RICK 
ID   B6Y9H2_9RICK            Unreviewed;      1556 AA.
AC   B6Y9H2;
DT   20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2009, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Nad-dependent glutamate dehydrogenase {ECO:0000313|EMBL:EEB55362.1};
GN   Name=gdhB {ECO:0000313|EMBL:EEB55362.1};
GN   ORFNames=C1A_1171 {ECO:0000313|EMBL:EEB55362.1};
OS   Wolbachia endosymbiont of Culex quinquefasciatus JHB.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=569881 {ECO:0000313|EMBL:EEB55362.1, ECO:0000313|Proteomes:UP000004540};
RN   [1] {ECO:0000313|EMBL:EEB55362.1, ECO:0000313|Proteomes:UP000004540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|Proteomes:UP000004540};
RX   PubMed=19114486; DOI=10.1128/JB.01731-08;
RA   Salzberg S.L., Puiu D., Sommer D.D., Nene V., Lee N.H.;
RT   "Genome sequence of the Wolbachia endosymbiont of Culex quinquefasciatus
RT   JHB.";
RL   J. Bacteriol. 191:1725-1725(2009).
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:EEB55362.1}.
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DR   EMBL; ABZA01000004; EEB55362.1; -; Genomic_DNA.
DR   RefSeq; WP_007302916.1; NZ_DS996942.1.
DR   HOGENOM; CLU_003404_1_1_5; -.
DR   Proteomes; UP000004540; 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   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          30..164
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          372..461
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          526..579
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          686..1172
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1219..1552
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1556 AA;  178445 MW;  D6B15C835A2E79BC CRC64;
     MCINHNVNVE SLFKLVDQGN KKEKEKIKEF IQYFYNFVYN SDLKVNDKFL LYIAEDAYNF
     ILKKEKEESK LAVSNVNDIS GIEGNFTIIK ITNYDMPFLV DSVISTIKSN GLTICYYSNS
     IINVQRKNSL IDKIHLLEES NGIKESVIYV IIKGISGSFV DTLEESLRKT LKAVNCVVKD
     WQLMLKKLLE HPALDAGGRD FLAWLKNNNF VFLGYQEYIT NKEGKLALSG KESLGLMRAS
     EEYQNSSIFS ESLNSLYILR SDLISIVHRR TYMNCIGVKE FNDQGDVIRE QHFFGLFTSI
     AEVQDIRTIP VIKDKVTTIE KKAGFVPGGH NNKALISILQ AFSCDELFQS NEDELFEICT
     SIMSLAIRPR VKLFLRKVGN FISCIVLIPM RYASARLMFK IRDILKDETN AESSDIYNNH
     IINEYDLMKL HVVLRTKSAS IFDDEVLRIE NKLRNITEKW EDRFIDNLYN TFSTVEDIFI
     RYCKAFPISY QENFEPHDAY YDMKKLEIVR KKKVSEVDLR LTRDNFNYQL KVYTPSNGGL
     ELSKILKVTK NLGAKILSHN GYYIEINGGI WIHHFVLSRV DELIDNITLK EQFEVTLVKV
     FSKEIKNDYF NSLIIIAGLE WKEVLLIRAL SAYLKQTSFS YNPEYIQKVV SEYPKVVRYL
     VELFHSRFDT KIDIDRAETT SILIEKIEEL LKEISNVSND YVLRSIFNLI MAILRTSYYQ
     DDKPYLSIKF DSSKINGLPD PRPYRELYVY SNLFEGIHLR GGKLARGGLR WSDRTEDFRT
     EVLGLMKAQM TKNAVIVPVG AKGGFVIKQV YKDKNISREK GVECYKNFIR GMLDITDNVV
     DGKITPPENV IRYDEDDPYL VVAADKGTAS FSDYANEISS ECNFWLEDAF ASGGSAGYDH
     KKMGITARGA WIAAQRHFWR MNKDIYQDTT VIGIGDMAGD LFGNGMLLSR NMSLIGAFNH
     MHIFVDPNPD AEKSFVERKR LFELPFSTWM DYNRDLISHG GGVFERSSKQ VEISQEMKKC
     FDITEDTLSP NDLIRYLLKA KVDFIWNGGI GTFVKAKSES HGMVGDKAND ELRVNGHDIR
     ASMFIEGGNL GCTQLGRVEY AKIGGYINAD FIDNSAGVIC SDLEVNIKIA FVAIMKEGGI
     FLEKRNEILA SMIDEVASKV LENHNRIETK ALLLECLQAK EKLEQHHKLL LSLEKFGLLN
     RDVEFLPAEE EVARMLTDGE GFCSPQLSVL MSYARTAIKN EVIHSELPEK DFLCRDYLLN
     YFPQRMVTEF KDSILKHQLC REIISTCITN DVVNRMGCIF INNLVESTGI KVHEAVNIYI
     VVNHLYNLSS LWQKIDELDG KIDVDSYLQV VRSVQKFIGR VSFWLVKNLG KLNLVELDGV
     TKFRGAIETL GHDILDDRLL KIYNHGLTSL VELNINKDLA KKVADLRILI YALDVISIAE
     QTSLSIFEAG RIYFKLKSLL RFDMIRTIAV KIKSHSSYWD RSLINDLLDD LSNYHHKLAV
     KVIKATDNHI DKVQTWALND KDYIERYNSF LDEMVASKLD LSKLILIIRR IKVLAS
//
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