ID Q1QXW3_CHRSD Unreviewed; 1612 AA.
AC Q1QXW3;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Glutamate dehydrogenase (NAD) {ECO:0000313|EMBL:ABE58695.1};
DE EC=1.4.1.2 {ECO:0000313|EMBL:ABE58695.1};
GN OrderedLocusNames=Csal_1340 {ECO:0000313|EMBL:ABE58695.1};
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE58695.1, ECO:0000313|Proteomes:UP000000239};
RN [1] {ECO:0000313|EMBL:ABE58695.1, ECO:0000313|Proteomes:UP000000239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11
RC {ECO:0000313|Proteomes:UP000000239};
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
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DR EMBL; CP000285; ABE58695.1; -; Genomic_DNA.
DR RefSeq; WP_011506641.1; NC_007963.1.
DR STRING; 290398.Csal_1340; -.
DR KEGG; csa:Csal_1340; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_6; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000000239; 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,
KW ECO:0000313|EMBL:ABE58695.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000239}.
FT DOMAIN 35..178
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 409..498
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 554..630
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 728..1222
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1268..1603
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1612 AA; 183362 MW; 437EDAEC7F6BE070 CRC64;
MQHVAIEGKE DFLAQLKEQL AKRLPQDKVQ RIAAFAEDLY ASAPFEEAAE RGLDDIYGAT
LSAWHFMQTH DPRDAKVRVF NADFEEHGWQ SPHTVVAVLH EDMPFLVDSV RIELNRRGLT
VHAIHNAVLA VERDAKHHLK RVTSTEAKDA PSARESIILV EVDRHSDAAT LDDLHEGLEE
VLRDVRAAVE DFDPMRDQVR QAIKELKAKR PKQIKADDHK EAIAFLEWLL DDHFTFLGYD
EYEVVQEDGQ DRLRQIPKSE LGVFKLDQPR YRERITTDEG IEDDQYVLVP ELLSFAKSAY
HARVHRPAYP DYISIDRYDE EGRVVGERRF LGLYTSTVYN ESPRNVPVLR KKIEAVIKAA
GVNPKGHNGK QLTQILEVYP RDDLFQIDTD ELARTVFGIL NIRERRKVRL FIREDRFGQF
YSCLAFVPRD VFSTELRVRI QNMLCEELDA TFGDFNTYLS ESVLARIQFI LRFNGERPAE
YDVRRLEKKI AALSRSWRDD LQSAMVEGYG EEQANRLMQQ YREAFPSSYR EDFSARTAVY
DIHHLSELDA PAPISLSLYR LVEENIDGVN LKLFHADHPI PLSDVLPVLE NLGLRVISER
PYDIQCPERT YWIHDFTLEH RGDGVVNLQE MRDVFIEAFT RIWTGDAESD AFNRLVIGAN
LAWREVAVLR AYARYLKQLR FGLSQDYIAN TLASHPEITR ELVTLFELRF DPDDTASEDE
VDECVARIEG LLDQVASLND DLLLRRYVAL IQATLRTNYY QQREDGEPKD YIAFKLEPTR
VPDMPKPRPM FEIFVYSPRV EGVHLRGGKV ARGGLRWSDR HEDFRTEVLG LVKAQQVKNA
VIVPVGAKGG FICKRMPEGA DRDVVQKEGI ACYQIFIRAL LDVTDNLEGG DVVPPERVVR
HDDDDPYLVV AADKGTATFS DIANAISLEY GHWLGDAFAS GGEHGYDHKK MGITAKGAWE
SVKRHFREMG LNTQETPFSV VGIGDMAGDV FGNGMLLSDK IRLVAAFNHR HIFVDPDPDP
AASFKERQRM FELARSSWED YDTSLISKGG GVFSRDAKSI TITAEMKKAF DIEAGKLSPN
ELIRAILVSR YDLLWNGGIG TYVKAADETH ADVGDKANDA LRVDGGELRC RVVGEGGNLG
LTQRGRMEAA EKGVRVNTDF IDNAGGVNCS DHEVNIKILL DDIVKRGDMT DKQRNQMLAE
MTEEVGELVL RDNYRQTQAL SLSEILSQQG MGPYRRFINE LEAAGGLDRE LEFLPSDEVL
IERANADKGL TLPELSVLIS YAKSALKTDL IASDLPDNPH VQRHMARAFP HTLVERFSDE
MYQHRLKREI TATQIANDLV DHMGISFVRR LRDSTGASRA EVARAYIIAR DCFNLEGLWE
QIEALDYQVD SQVQYGMMLD LMRLLRRATR WFLRHRTSQG IQEAIEYFAP RVTQLQENIG
KRLRGEDRET WDTRRDELEK AGVPQRLASV IAAAGSLYAG LGIIEAARAT DEKVQRVAEV
YYEIGHRLEL PWMNGQINAL KVRDSWQAQA RETFRDDLDR QQLALSISVL KMEGAPRDVE
PRVDQWLERH AGLVERWCGL LDEVRSGSQG GFPLFAVAIR ELVDLAESNG EG
//
