ID J3ATM4_9PSED Unreviewed; 1630 AA.
AC J3ATM4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:EJM71403.1};
GN ORFNames=PMI31_04058 {ECO:0000313|EMBL:EJM71403.1};
OS Pseudomonas sp. GM55.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144333 {ECO:0000313|EMBL:EJM71403.1, ECO:0000313|Proteomes:UP000007268};
RN [1] {ECO:0000313|EMBL:EJM71403.1, ECO:0000313|Proteomes:UP000007268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM55 {ECO:0000313|EMBL:EJM71403.1,
RC ECO:0000313|Proteomes:UP000007268};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM71403.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKJJ01000076; EJM71403.1; -; Genomic_DNA.
DR RefSeq; WP_008020058.1; NZ_AKJJ01000076.1.
DR PATRIC; fig|1144333.3.peg.3957; -.
DR Proteomes; UP000007268; 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 35..178
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 407..496
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 552..631
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 733..1227
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1272..1609
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1630 AA; 183134 MW; 5797226648034C57 CRC64;
MAFFTAASKA DFQHQLQAAL AQHISEQALP QVALFAEQFF GIISLDELTQ RRLSDLAGCT
LSAWRLLERF DHAQPQVRVF NPDYERHGWQ STHTAVEVLH HDLPFLVDSV RTELNRRGYS
IHTLQTTVLS VRRGSKGELL EILPKGTQGD DILQESLMYL EIDRCANTAE LTVLSKELEQ
VLGEVRVAVG DFEPMKAKVQ DILTKLDNSQ FAIDADEKSE IKSFLEWLVG NHFTFLGYEE
FVVSDEADGG HIVYDKDSFL GLTKLLRAGL SYDDLRIEDY AVNYLREPTL LSFAKASHPS
RVHRPAYPDF VSIREVDANG KVIKECRFMG LYTSSVYGES VRVIPYIRRK VEEIERRSGF
QAKAHLGKEL AQVLEVLPRD DLFQTPVDEL FSTVMSIVQI QERNKIRVFL RKDPYGRFCY
CLAYVPRDIY STEVRQKIQQ VLMDRLKATD CEFWTFFSES VLARVQLILR VDPKNRLDID
PLLLEKEVVQ ACRSWQDDYA ALTIESFGEA HGTNVLADFP KGFPAGYRER FAAHSAVVDM
QHLLSLNEKN PLVMSFYQPL GQVSGQRMLH CKLYHADTPL ALSDVLPILE NLGLRVLGEF
PYRLRHNSGR EFWIHDFAFT AAEGLELDIQ QLNDTLQDAF VHIVRGDAEN DGFNRLVLTA
GLPWRDVALL RAYARYMKQI RLGFDLGYIA STLNNHTDIA RELTRLFKTR FYLARKLTGD
DLEDKQQRLE HAIHSALDDV QVLNEDRILR RYLDLIKATL RTNFYQTDAN GHNKSYFSFK
FNPHLIPELP KPVPKFEIFV YSPRVEGVHL RFGNVARGGL RWSDREEDFR TEVLGLVKAQ
QVKNSVIVPV GAKGGFLPRR LPLGGSRDEI AAEGIACYRI FISGLLDITD NLKDGALVPP
ANVVRHDDDD PYLVVAADKG TATFSDIANG IAIDYGFWLG DAFASGGSAG YDHKKMGITA
KGAWVGVQRH FRERGINVQE DSITVVGVGD MAGDVFGNGL LMSDKLQLVA AFNHLHIFID
PNPDPATSFA ERQRMFDLPR SAWSDYDTSI MSEGGGIFSR SAKSIAISPQ MQERFDIEAD
KLTPTELLNA LLKAPVDLLW NGGIGTYVKA SSESHADVGD KANDALRVNG NELRCKVVGE
GGNLGMTQLG RVEFGLNGGG SNTDFIDNAG GVDCSDHEVN IKILLNEVVQ AGDMTAKQRN
ELLASMTDEV GGLVLGNNYK QTQALSLAAR RALPRIAEYK RLMNDLEGRG KLDRAIEFLP
AEDAINERIA EGHGLTRPEL SVLISYSKID LKEQLLGSLV PDDDYLTRDM ETAFPPTLVS
KFSAAMRRHR LKREIVSTQI ANDLVNHMGI TFVQRLKEST GMSPANVAGA YVIVRDIFHL
PHWFRQIENL DYKVSADVQL ELMDELMRLG RRATRWFLRA RRNEQNAARD VAHFGPHLAA
LGLKLDELLS GEIRETWQTR YQAYVEAGVP ELLARMVAGT THLYTLLPII EASDVTGQDP
ADVAKAYFAV GSALDITWYL QQISALPVEN NWQALAREAF RDDVDWQQRA ITISVLQQGN
GTLDVETRLE LWMEQYEGMI ERWRAMLVEI RAASGTDYAM YAVANRELLD LALSGQAVVP
AAVAAELEPA
//
