ID A0A109LPP1_9SPHN Unreviewed; 1578 AA.
AC A0A109LPP1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KWV91510.1};
GN ORFNames=AUC45_09730 {ECO:0000313|EMBL:KWV91510.1};
OS Erythrobacter sp. YT30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1735012 {ECO:0000313|EMBL:KWV91510.1, ECO:0000313|Proteomes:UP000055668};
RN [1] {ECO:0000313|EMBL:KWV91510.1, ECO:0000313|Proteomes:UP000055668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YT30 {ECO:0000313|EMBL:KWV91510.1,
RC ECO:0000313|Proteomes:UP000055668};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. YT30.";
RL Submitted (OCT-2015) 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:KWV91510.1}.
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DR EMBL; LMAF01000002; KWV91510.1; -; Genomic_DNA.
DR RefSeq; WP_067601680.1; NZ_LMAF01000002.1.
DR STRING; 1735012.AUC45_09730; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000055668; 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:UP000055668}.
FT DOMAIN 74..162
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 380..467
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 531..601
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 706..1195
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1240..1560
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1578 AA; 172622 MW; A3FE9F5B944660B8 CRC64;
MAKKQAASSS EKAAKINSSA ADQALLKPLK QHLAASVLPG DTPLEGDELE DVAHYLLLAG
EKRTPARSTL KLQSTTGERR RLKIAVINDD MPFLVDSIAS TITAHGLSID RLVHPVIETT
RNDEGQLTAL AKPREDADGS LPESFIYIET PRVDARQRSE LLSDLKTTLG DVRAAVSDWP
KVQKAMQRDI SAIGGSSPEA AALLTWLNNG MLTQLGHVTQ NRDGSTAKAR GICRKSAQPI
LSETSFDRAF QWFDDSPKDA PARDLLVIKS NRQSTVHRRI PLDLFIVPVR EDGKTSSLSV
HAGVWTSAAL ATRPQDVPVL RASLAQLTTN LGFDRTGHAG KALVHAFTAL PHDLLVAFGP
DDIQRLTTAM MSLVDRPRPR LVLVNSALGR HVFAFVWLPR DMLNTETRLQ IEDLLTDESG
ASVLSWSLEV EGSTLAMLQF LLDTRETDTV PDADKIEAQL EELLRGWGDA VENELSKIED
NGRANAIATR YADAFPPAYR SDYGAKEAAR DISRLRALAS SGDEQSDQRD ARLYRLDTDK
DDVFRLKIAH IGGSLSLSDA VPAFENFGFR VITERNIALD GGSLGTIHDF TLKLANEAKI
DALLDRSSII ECAIAEVLNG GSEDDPFNRL VVEAELGVRE AVWLRAIYRY LRQTGMSFTI
YTVVDALSAA PSVTRAMIDM FTACHDPEFD GDRDKALEEA KDAFGKGLTK VSAINDDRLL
RLYRAVIEAV LRTNAFAEAA NEALAFKIES EKVPYLPKPV PWREIFVYSR RVEGIHLRSG
VIARGGLRWS DRRDDFRTEV LGLMKAQRVK NAVIVPTGAK GGFYPKQLPN PSQDRDAWAK
EGKESYKVFI RSLLSVTDNL KGNKVVHPED VVIHDGEDPY FVVAADKGTA SFSDVANGIA
EDKNFWLGDA FASGGSNGYD HKAMGITARG AWVSVQRHFL EMGIDVQEDT IEVVGCGDMS
GDVFGNGMLL SKAIKLVAAY DHRHIFIDPS PDPAASWKER KRLFEKSSSS WDEYDKDLIS
RGGGVYSRDA KNITLSKTAA SMLGLECEEI TPDNLVSAIL RAPVDLIWFG GIGTYIKSED
ESNSDVGDRA NDALRINARQ VGAKVIGEGA NLGITQAGRI EFALNGGRLN ADFIDNSAGV
DCSDNEVNIK IALASAVRGG DLTEKKRNNL LQKMTDEVAE IVLEDNRLQA LALSIAEAAG
AKAMDSYIRL IERLEEMGVL DRENQGIADN EMLKRRANDG KGLTRPELAV LLSTTKLVLQ
DAIEESDLPD DPSLEDDLIN MFPEPMRKDF KGAITDHRLR RELIATELAN RIVNSMGPLA
VFELAEEEGA MLEAIAKTFV AVDTLFDMRG LWTQIDDAKV SEATRIELFE RTGQALGAHM
GDLLRAGAAR QRASELAEEL APGINELTKA TETLISGDAR QQSDNMRGEL TDAGTPKELA
GQIVRLFEMD GAAGLARLAQ TSGLPITDLT SAFTDLGARL GLDWAQRTAA LMEPSDVWER
MLVAGLARDF QQMRLDLLRA LLKKKDAEPK SAVDKWADDN SASIRQFRNV VARAQNQTPV
APAVLAQIAS QARGVLEA
//
