ID W1N4G9_9GAMM Unreviewed; 1616 AA.
AC W1N4G9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:ERL50423.1};
GN ORFNames=BJB45_04640 {ECO:0000313|EMBL:ERL50423.1};
OS Halomonas huangheensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL50423.1, ECO:0000313|Proteomes:UP000019113};
RN [1] {ECO:0000313|EMBL:ERL50423.1, ECO:0000313|Proteomes:UP000019113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL50423.1,
RC ECO:0000313|Proteomes:UP000019113};
RA Miao C., Wan Y., Jin W.;
RT "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:ERL50423.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AVBC01000039; ERL50423.1; -; Genomic_DNA.
DR RefSeq; WP_021820474.1; NZ_CP013106.1.
DR STRING; 1178482.AR456_06060; -.
DR PATRIC; fig|1178482.3.peg.3526; -.
DR eggNOG; COG2902; Bacteria.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000019113; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019113}.
FT DOMAIN 36..178
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 410..499
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 555..631
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 729..1224
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1270..1607
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1616 AA; 183326 MW; A6263FBA23B3DC65 CRC64;
MLHVAQDDSR EDLLNQLEER LQGRLEQDRA DQVIDFTRLF YSSVPFEDLA ERRQDDLYGA
TLSVWHFLQQ FDADAPKVRV MNPDFEEHGW QSTHTFVAVL HRDMPFLVNS VRMELNRRGM
TVHAIHNSVL AVERDAQHRV TRVASPRDAD APEARESLIA IEVDRHSDPE ELTAIEDSIQ
EVLREIRTAV GDFHDMRQKV SDSIDELKAS CPANINAEDH QEAIAFLEWM LQENFTFLGY
DEFTIEGSGT RQKLVTVQGS ELGLLSLEDN EYRQRIRTDE GLEDGRYVLV PQLLSFAKSA
RHARVYRPAY PDYITVDRYD EAGNVIGERR FLGLFTASVY NDSPRHVPLL RRKLKAVMEI
AGFNPKGHNG KQLIQILDVY PRDDLFQIHT EELARTAVGI LDIRERRRVR LFVREDRCGK
FYSCLVFVPR DVFSTELRIR IQELLCEEFD ASFGDFNTHL SESVLARIQF ILRFNGDKPV
EYDIKALETK LARLARNWRD DLLNAAIEGF GEEHANLVLR DFRDAFPASY REDFSARTAV
YDLQHIGELD SGSSLSLSLY RLVEEEGSGV NLKLFHKDTG IPLSDVLPMM ENLGLRVLGE
RPYCVEAEER NYWIHDFDLE HHTATEVNLQ EMRETFIDAF QRIWAGEADN DRFNRLVIGA
NLGWREVAML RAYARYLKQI RFGISQEFIA NALVAYPHIT RELVTLFELR FDPEERPADS
EIDACVERIH GMLDDVASLN DDRLLRRYVE LIQATLRTNY YQRAEDGSYK DYLSIKLQPS
KVTGIPKPRP MFEIFVCSPR LEGVHLRGGK VARGGLRWSD RLEDFRTEVL GLVKAQQVKN
SVIVPVGAKG GFVCKRMPDG ADRETTQKEG IACYQIFIRA LLDVTDNLVG GEVVPPKNVV
RHDENDPYLV VAADKGTATF SDIANAISVE YGHWLGDAFA SGGANGYDHK KMGITAKGAW
ESVKRHFRGL GINTQTDEFT VVGIGDMAGD VFGNGMLLSE TIRLVGAFNH LHIFVDPDPV
DAAANFAERK RLFDMPRSSW EDYNRELMSE GGGIFSRAAK SVSISPQMKQ RFAISEDHLA
PNDLIQAMLR SEVDLIWNGG IGTYVKSSEE TDTDVGDKAN DALRINGRDL NCRVVGEGGN
LGLTQRGRME AAAKGIRVNT DFIDNAGGVN CSDHEVNIKI LIDEVVANGD MTDKQRNLLL
AEMTEEVGDL VLLDNYRQTQ ALDLSELLSH QGIGPYRRFI SELEAAGQID RELEFLPSDE
ELQERAANDQ GMTLPELSVL VSYAKSTLKG DLIASEVPDD PLVMQHVERV FPSVLIDRYH
DQVYNHRLKR EIVATQLAND LVDHMGIVFV RRLIDSTGMG RADIAHAYVI ARDCFQLPRL
WDQIEALDNK VATGVQYSMM LDLMRMIRRA TRWFLRHRTT MGSATDCIDY FAPRIAQLQE
KIGSRLRGED LETWETRRRE LTDAGVPEAL ANTVAAAGSL YAALGIIQTA RQVNEKPQRV
AEVYYEIGAR LELPWMVQQV NALPVKDSWQ AQARETYRDD IERQQMAVTA SILQMEGGSR
DISARVDQWL EYHVVMHQRW CKLLEQVGSG GNQGGFPLFA VAVRELVDLA ESNRES
//
