ID A0A125QKT0_9SPHN Unreviewed; 1562 AA.
AC A0A125QKT0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KWV94932.1};
GN ORFNames=ASS64_06990 {ECO:0000313|EMBL:KWV94932.1};
OS Erythrobacter sp. AP23.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=499656 {ECO:0000313|EMBL:KWV94932.1, ECO:0000313|Proteomes:UP000058666};
RN [1] {ECO:0000313|EMBL:KWV94932.1, ECO:0000313|Proteomes:UP000058666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP23 {ECO:0000313|EMBL:KWV94932.1,
RC ECO:0000313|Proteomes:UP000058666};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. AP23.";
RL Submitted (NOV-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:KWV94932.1}.
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DR EMBL; LNBY01000015; KWV94932.1; -; Genomic_DNA.
DR RefSeq; WP_067692381.1; NZ_LNBY01000015.1.
DR STRING; 499656.ASS64_06990; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000058666; 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}.
FT DOMAIN 65..150
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 362..449
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 514..580
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 686..1177
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1222..1550
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1562 AA; 170802 MW; E4B074628394D064 CRC64;
MGSRTAALPK KLQNAITERM RLSLLTGDTP FEKERLGDAA AFVGELAAQR TLGRSAMAIE
SISDERRLTR IAIINDDMPF LVDSVAATIA ALGLSIDRLV HPVIPVERDD AGKLIEIPDG
DPDDAYWESM IYIEAARVDA KTRRQLQESL KETLADVRAA VSDWPKMQDA MAADAKRIAA
ADSEGAELLD WLNSGMLTQL GHVKRYRDGR QEDEFGICRK SAAQLLAEAS YERAFAWFEA
DGDRRRPLII KANRLSNVHR RVPLDLFIIP VGEPGKPAAL SVHAGVWTSA ALAAAPRAVP
RLRRELETLR ERHGFDDTGH AGKALVHALT TLPHDLLIGF SEGDVERVAT TMMSLVDRPR
PRLALVEAPL ARHLFAFVWL PRDMVATQVR LEIQALLEEA ASARLLDWSL EVEGGNLATI
RFVLDIRDGD KAPDEARLEQ QMQTLLRGWS EAVEAELATI EEPSRAAGLA MRFADSFPTA
FRGRYGPREA ALDIARLHDL GASAENDDVV RGARLYFCER ELPGCLRLKL YQSEGSLPLS
EGVPALEDFG FYVRSEMPTV LDEGRLGTVH DFLLDLKPGA DPKALIERSD AIEEAVAAVL
NGEAENDPFN RLVPEAGLAA REANWLRAFY RYLRQAGMGF TIYTVVDALA AAPDVTRALI
ALFTARHDPE FGSGREKAIE EARSAIKRGL FKVKAINDDR LLRLYNSLID AILRTNAFAP
AAAEALAFKI DSAKVPGLPK PIPYREIFVY SRRVEGIHLR SGPVARGGLR WSDRRDDFRT
EILGLMKAQR VKNAVIVPTG AKGGFYPKQL PSPAIDREGW AAEGRGSYET FIRTLLSVTD
NIVDDKVVHP DQVVITDGED PYFVVAADKG TATFSDIANA IAQSRDFWLD DAFASGGSKG
YDHKAMGITA KGAWVSVQRH FLELGVDVQS DSIEVVGCGD MSGDVFGNGM LLSKAIKLVA
AFDHRHIFLD PDPDPAASWK ERKRLFGLQR SSWQDYDEKL ISKGGGVFPR DAKSIKLSKA
VQAKLGIEQS EIEPEALISA ILRAPVDLIW FGGIGTYIKA AQENNVQVGD PANDALRVDA
CAVQAKVIGE GANLGITQAG RIEFSLHGGR CNTDFIDNSA GVDCSDNEVN IKIALAAAKR
SGKLSERKRV ALLESMTDEV AQIVLEDNRL QALALSIAEQ GGAVAVPPQL RLIEALEDRG
ALDRQTEGLA SSENLGRRAS DGQGLTRPEL AVLLSSTKLV LQDAIEQSSL PDDPSVAGLL
VDYFPSAMRK KFKQQIETHQ LRREIVATAL ANRFVNRMGF VHPFELAEEE GVGLADVTAA
FVAADQLFGA GDLWEELETA AMPEDVRIYL FRHTAGALRS QMADLIRTGI SSEPPSKIIA
SLKDRVARLM TGSEELLTAA SIRQSDRLKA EFVDMGAPEK LAARVTHLYQ IDGAVGLAAL
SRAAEIEVRA LTAAFTDLGE RIGLDWAQST SAMMNPSDVW ERLLVAGLSR DFQQMRLEFL
RRLSRRKGAK KDPIGAVAGW ADEHAAAIRR FRAMVGRAQA QSEVAPAMLA QVASMARNLL
AR
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