ID M2YGC0_9MICC Unreviewed; 1633 AA.
AC M2YGC0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=NAD-specific glutamate dehydrogenase, large form {ECO:0000313|EMBL:EME37575.1};
GN ORFNames=C884_01626 {ECO:0000313|EMBL:EME37575.1};
OS Kocuria palustris PEL.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME37575.1, ECO:0000313|Proteomes:UP000009877};
RN [1] {ECO:0000313|EMBL:EME37575.1, ECO:0000313|Proteomes:UP000009877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEL {ECO:0000313|EMBL:EME37575.1,
RC ECO:0000313|Proteomes:UP000009877};
RX PubMed=24504000;
RA Sharma G., Khatri I., Subramanian S.;
RT "Draft Genome Sequence of Kocuria palustris PEL.";
RL Genome Announc. 2:e01261-13(2014).
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:EME37575.1}.
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DR EMBL; ANHZ02000003; EME37575.1; -; Genomic_DNA.
DR RefSeq; WP_006213700.1; NZ_ANHZ02000003.1.
DR STRING; 71999.KPaMU14_01130; -.
DR Proteomes; UP000009877; 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 Reference proteome {ECO:0000313|Proteomes:UP000009877}.
FT DOMAIN 32..182
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 409..497
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 563..625
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 743..1240
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1289..1628
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1633 AA; 182362 MW; CF2FD473A41A61EE CRC64;
MAESQDRPDP STADAQDSGG RRHPRPGSEP WMRTYYAGAP AQDLDRRGED VLAARAQRHR
ELAQHRERGE VLITTLDEGS RTVVLIVADD VPYLVSTLNA RIAGDWGGAR LVVHPILRAT
RDDDGELRSV DELEDVRAIS SGDTQTIPIV GALGETSAAE SWIQVELAEH LDESQAQELI
EGLRPALRTV AQIDADHDDM VRWVGSVNDS LSPMRSQLDD VEPAQEFLTW LLDGRFVLMG
VKEYDLREDD EGLYLSSVEG SGLGILTETE EKSGRPRRLT VQAAEHARDR QAMFVTKANT
RSGLHRNDYL DYIGVRRFDA DGQVDGEYLI LGLFARKAYS TSARNTPWVR DKVRAVAESF
GFRPDSHSER DLQSVLEEYP RDELLHMSVE EAVRAARGVV ELDERRVTRL FCRTDLFGRF
VSAVVYLPRD RYNTEVRERI SEILTEAYGA VDVDFDVSLS TSSLARLFFR LRLPQDTPPP
VDHEDLQLKV RKAARSWPEA LSMEIEELFD SERAREYVQR WAEAFPADYR AHYEIDEAIE
DLRRCEMLWG RDEALPAEVR VAPSTAEGEP VRVNVYLTRS LTLTEMLPME QNLGLTVLDQ
KPYQIRTGDG REFQLYDFGV ELPDGVDAVG PDDARTEDLI EEILCAVISG RSESDSLDRL
VLAERMHWRS IAVLRAYVKY LLQLRVPHSF EFMSDTLLAQ PQVTRGIVEL FETSFDPQRF
AGEDGQPDDE AREAARAEVL EKLEAALDEV PSLDADRFLR TLVEVVCATA RTNAYQQDRP
AIALKLEPRR ISAAPLPRPR HEIWVWSPRV EGTHLRFGPV SRGGLRWSDR REDFRTEVLG
LVKAQMVKNS VIIPDGAKGG FFPKQLPDPA QDRGAWGEAG KDAYKEFIGS LLDVTDNLVP
QEDGEDRVVV PEAVVRRDGD DSYLVVAADK GTAKFSDTAN AISLERGFWL GDAFASGGSV
GYDHKAMGIT ARGAWESVKR HFFELGHDTQ TQDFTVVGVG DMSGDVFGNG MLLSEHIKLV
AAFDHRDIFL DPDPDPAASF AERKRVFEMG PSSWKDYDAS LISDGGGVHS RSSKSIPVSE
RVREVLGLPE GTTEMAPPEL MRAILKAPVD LFYNGGIGTY FKASTETNAD VGDKANDAIR
VNGADVRVRV IGEGGNLGAT QLGRIEAAQN GVLINTDAID NSGGVESSDR EVNIKILVDR
MVAAGELPQD ERAGFIESMT EELASLVLRT NVAQNITLSV DRWKADDYAL TYARFMDWLE
ENADLDREIE YLPTDEQLEA RAEDPEIDEP LTAPELSVLT AYAKIQLSGE LIRSDLAEDP
WTARIVQRYF PEAMGERFGE DLQTHPLRRE IVGTLVANQM INMGGATFAY RALEQTSCEP
GELAAAFLAA VEIFELDPLL QQLAELPADV STEQWIQMIQ DVRRLLDRAV RWLISRGLSQ
QPVEQVVEAF AQIPEVRREG LTFLGAEDAE AAQRREQLAL EQGISEELAQ TWSRLLDSYS
LLDIVRLAES EGEDQDLELV GQLYFALHER FGIQTMLTRI SGLPQTTRWE VLARMSMRED
VYSTLTSMTA MALRADGETA EQKVEAWIEE NRQSLERVGR TLQEIESSSG GDAATDMAAL
SVALRSMRSL ISA
//
