ID B9Z8N1_9NEIS Unreviewed; 1603 AA.
AC B9Z8N1;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=NAD-glutamate dehydrogenase {ECO:0000313|EMBL:EEG06814.1};
GN ORFNames=FuraDRAFT_3718 {ECO:0000313|EMBL:EEG06814.1};
OS Pseudogulbenkiania ferrooxidans 2002.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Pseudogulbenkiania.
OX NCBI_TaxID=279714 {ECO:0000313|EMBL:EEG06814.1, ECO:0000313|Proteomes:UP000003165};
RN [1] {ECO:0000313|EMBL:EEG06814.1, ECO:0000313|Proteomes:UP000003165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2002 {ECO:0000313|EMBL:EEG06814.1,
RC ECO:0000313|Proteomes:UP000003165};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Coates J.D.;
RT "Sequencing of the draft genome and assembly of Lutiella nitroferrum
RT 2002.";
RL Submitted (FEB-2009) 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:EEG06814.1}.
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; ACIS01000014; EEG06814.1; -; Genomic_DNA.
DR RefSeq; WP_008955735.1; NZ_ACIS01000014.1.
DR eggNOG; COG2902; Bacteria.
DR Proteomes; UP000003165; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 35..176
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 405..494
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 550..622
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 725..1219
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1265..1598
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
FT COILED 711..738
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1603 AA; 180467 MW; C6B3576E84785926 CRC64;
MSLSNMTEHA SLIDDIQAEA DSKLSSDEQQ KLAPFFPVYF EEAEYDDLRR YSSLDLFGAA
IAHYDFAQQR KPGAHKARIY NPDFERDGWQ STHTVIEVVG DDMPFLIDSL AMLLSRYNLN
LHLLIHPVVA VARDAKGQLV ELKRTQGRDL PLESWIHVEI DRVSDAATLK RLESDLNRVI
SDIRLVVNDE PKMRAALSEI ADDLAKVKGA RGDEAREAID FLHWMGNNHF LLMGYCDYDL
VKRDGKDSLK IIKESGLGIL KEQGDKEYSA SFEQLPQELR ELAHLPQLII LNKSQTRSII
HRPAYIDFVG IKRFNSKGEV IGERRFLGLY TAHAYQVSLK NIPIVRRKAE YVVNYCDYVD
NSYKAKTLGF VLENYPRDEL FEIPAETLAP IIEGIVNLQE RPRVRLFVRT DRYHRYVSCL
VYVPRDSFNT EVRLKIEKVL LNAFNGTAAE FSVQIGDGTL ALVHYTIRTH AAGLPAFHES
DIEAEIARVV RGWQEELHQL LVEAHGEEQG NSLFHRYKGA FPVAYREEFA ARNAVLDIQL
MQSLGGEKRL GMKLYRPLHR GTNAFNLKLF SAGEPLGLSA SLPILENMGV RVRDEHPYRV
QRSDGAEVWI SDFGLDVGSA YEQMATDDVQ HDFQELLSQV FAKRCENDGF NRLALVAGLD
WREISLVRAL AKYLRQGGLT FSQAYIEQCV ANYPAITRNL VSLFQARLDP VNADDAQAET
LQAELKNLLD KVANLDEDRI LNGFLSVILA VRRTNFWQKA EDGQFKSYIS FKLESNAIPF
LPQPRPMFEI WVYSPRVEGV HLRGSKVARG GLRWSDRMED FRTEVLGLVK AQMVKNSVIV
PMGSKGGFVC KQLPPASDRE AFMAEGIACY KTFISALLDV TDNLVTGQIV PPKEVRRLDP
DDPYLVVAAD KGTATFSDIA NGISEQYGFW LGDAFASGGS AGYDHKGMGI TARGAWESVK
RHFRHLGVNT QEQDFTVIGI GDMAGDVFGN GMLLSEHIQL IAAFNHMHIF LDPTPNAAVS
FAERARLFNL PRSSWADYNR ELISQGGGIF ERSAKSIPLS PEVKAWLETD KDSMAPNELI
HEILKARADM LYNGGIGTYV KASTQSHADA RDRACDPVRV DGRELRVKVV AEGGNLTCTQ
LGRVEFALSG GRICTDAIDN SAGVDCSDHE VNIKILLGAV MQAGDMTLKQ RNELLAEMTE
EVGHLVLRNN YLQTQVLAIK QQEAASILST HARMIVHMEK TGELNREIEY LPSEAQINDR
RLARQGLTAP EVAVLLAYSK ISLDQAILAT DVPDDVDFLP VLVNYFPKPL QEGFRGQMEK
HHLKREIISN QLANQIINRM GTTFVFRLQE ESPFSAADIA RAWWIASRVF NAEQLWGQIE
ALDNQIPADQ QMELMVIVRT LIERVTRWVL RNKRPFSSVN AVIDQYGAKV QALLAALPEL
ISATDYPTVA AMEARLDIPN LPASLARVLA RLEFAVPLMD IIEIGEGEEL TQGVLASNYY
RLGKVLQLDW MREAITRLPR DNRWQSLARS ALRDDLYRLH RKVAKLAIQE CKESEDLASA
WLEKRHHDVE TCHQMFAELQ AFQALDLAML SAGMRELNNH LLA
//
