ID A0A074MTA6_ERYLO Unreviewed; 1565 AA.
AC A0A074MTA6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glutamate dehydrogenase {ECO:0000313|EMBL:KEO88877.1};
GN ORFNames=EH31_15710 {ECO:0000313|EMBL:KEO88877.1};
OS Erythrobacter longus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO88877.1, ECO:0000313|Proteomes:UP000027647};
RN [1] {ECO:0000313|EMBL:KEO88877.1, ECO:0000313|Proteomes:UP000027647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO88877.1,
RC ECO:0000313|Proteomes:UP000027647};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL Submitted (APR-2014) 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:KEO88877.1}.
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DR EMBL; JMIW01000007; KEO88877.1; -; Genomic_DNA.
DR RefSeq; WP_034961708.1; NZ_JMIW01000007.1.
DR STRING; 1044.EH31_15710; -.
DR eggNOG; COG2902; Bacteria.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000027647; 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:UP000027647}.
FT DOMAIN 39..150
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 363..450
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 513..582
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 691..1180
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1225..1548
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1565 AA; 169376 MW; 291357D8C4A3278E CRC64;
MSVKSDASSK ASKASPKTLK QALSKHLVAS ILPGETKIEK SDLDGAVEFL LVAAQKRASS
SSVIHHESDT SERRLRIAII NDDMPFLVDS IAATITASGL GIDQLLHPIA PVTRDEDGLL
TAIGDKDAFK ESLIYIETPR VDAKQRRALL SDLRNTLEDV RAAVSDWPKM RSVMARDAQA
LGESDSAKLL DWLNGGMLTQ LGSLTRTRDG ETSDALGICR KSAKAILADA SFERAFEWFE
KGGPDRKLLA VKANQVSNVH RRTPLDVFLV PVREGKKLTA LSVHAGVWTS AALAAPPSKV
PIIGNALATM TADLGFDPRG HAGKALAHAF SALPRDLLVS FEEKDITRLV SAMMSLVDRP
RPRIILVQSP LGRHVFAFVW LPRDYLSTQL RQQIQALLTE ATGLDLLSWN LQVDGGSLAM
LQFLLDSRSI AKMPDAEAIE AQLEDLLKGW SEAVETHLAK GNDSARVAAI TQRYAEAFPP
GYRLRYGAAE AARDITQLHA IATSEAPEAR SCRLYKLDND TRGDLRLKIY HVEGRVALSD
AVPVLENFGF RVLSEVPTRL EGGTLGTIHE YTLIAPQGAS IDGLIERADA IENAIAEVLN
GHSENDPFNR LVVANGLGAA QTVWLRAIYR YLRQTGANFT IYPVVDALER ASDVTAAMVD
LFTARHDPDL AGATSDEREM AIKSAITAFT RGLAKVSAIN DDRLLRLYRA VIDAMLRTNA
FAPAAEEALA FKIDSALVPG LPKPVPWREI FVYSRRVEGI HLRSGAVARG GLRWSDRRDD
YRTEILGLMK AQKVKNAVIV PSGAKGGFYP KELPSPAIDR DAWAAEGRAS YQVFIRTLLS
ITDNIVNGKV VHPKAVRVHD GEDPYFVVAA DKGTATFSDV ANGIAADAGF WLDDAFASGG
SNGYDHKAMG ITARGAWVSV QRHFLEMGVD VQKDSVRVAG CGDMSGDVFG NGMLLSKAIQ
LVAAFDHRHI FIDPDPDPAT SWKERKRMFD LPRSSWEDYN PALISKGGGV FSRAAKSIKL
SKKARTMLGI EEKEIGPDDL ISAILKAQVD LLWFGGIGTY IKAESENHIE VGDPANDTLR
VDAREVGAKV IGEGANLGIT QAGRIAFSLN GGRINTDFID NSAGVDCSDN EVNIKIALAA
ATRDGAITTP KRNTLLAQMT DEVGEIVLED NRLQALALSI AEAGGAEASA SYIRLIESLG
EMGALDRRTE GLGDSETYMR RAADGKGLTR PELAVILSST KLALQDAIEA SGLPDDPVLE
SNLIDLFPKP MQSKYVSYIR DHQLRRELIA TDLSNRIVNR LGLIHAFELP EEEGVGLSDV
AAAFVVVERL YDLKTLWADI DASTMPEPAR ITLLERAAAA VGNLMSDVLR TTGGRVEAGA
MVAELNAGVD VLNKQRESLL SGDTLDRSNA LRASFIEQGA PADLAGKVAD LFDYDGSVGL
ASLALKAGID PAVLTQAFGD IGRRIGIDWA QGVAAHMSPS NVWERLLVDG LARDFQHMRI
EFLRRLTRRK GGKDDPQGAI ASWAETNARA IVQFRSMIAR AQNAPPVAPA ALAQIASQAR
NLLER
//
