ID   F4QJQ0_9CAUL            Unreviewed;      1639 AA.
AC   F4QJQ0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Bacterial NAD-glutamate dehydrogenase family protein {ECO:0000313|EMBL:EGF92001.1};
GN   ORFNames=ABI_04330 {ECO:0000313|EMBL:EGF92001.1};
OS   Asticcacaulis biprosthecium C19.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF92001.1, ECO:0000313|Proteomes:UP000006512};
RN   [1] {ECO:0000313|Proteomes:UP000006512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA   Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Draft genome sequence of Brevundimonas diminuta.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL883077; EGF92001.1; -; Genomic_DNA.
DR   RefSeq; WP_006271170.1; NZ_GL883077.1.
DR   STRING; 715226.ABI_04330; -.
DR   eggNOG; COG2902; Bacteria.
DR   HOGENOM; CLU_003404_1_1_5; -.
DR   OrthoDB; 9758052at2; -.
DR   Proteomes; UP000006512; 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; 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; 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          44..175
FT                   /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT                   /evidence="ECO:0000259|Pfam:PF21075"
FT   DOMAIN          421..509
FT                   /note="NAD-glutamate dehydrogenase ACT2"
FT                   /evidence="ECO:0000259|Pfam:PF21076"
FT   DOMAIN          575..652
FT                   /note="NAD-glutamate dehydrogenase ACT3"
FT                   /evidence="ECO:0000259|Pfam:PF21077"
FT   DOMAIN          752..1252
FT                   /note="NAD-glutamate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF05088"
FT   DOMAIN          1297..1633
FT                   /note="NAD-specific glutamate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21074"
SQ   SEQUENCE   1639 AA;  181173 MW;  772731717092FCC9 CRC64;
     MDELTTAGAS GDTLHTVKDA LTRGFVSATG HRDFLRLPDA EKVFLAQILE DFDPEELPGL
     DTASLNAIIA GFWSFGDSRA HGTETLRRIR PVTTSAGEGT AYDLIEIVQS DSPFIVETVM
     GELIDQGVSI RSMFHPVVTA ARDGNGRRAA TGTATKESMM LIVIERQSAD RHKAILSGID
     ASLHDLKLAV LDFPRMQKLL AEEIATLAKL RDDKTIKVDD AVLAENLAFL HWVDENHFVF
     LGARGYTYPR SDDGAYVQEQ PMNQLQEGFG VLRDPNRLIL RRSSEPAVLS AQILHQLENS
     EPVTVAKANI KSRIHRRVYM DYVGIKRYGA DGKPAGEVRF VGLFTSEAYD RPAFEVPLVR
     RKAQHVLHEA SVMGLQGGYN EKRLKNIVET YPRDELFQMT EDELLRTARG ILHLSDRPRV
     KLFTRKDPFD RFISVMLYIP REIYQSQMQI KAGEILAAAY LGRVSASYPY INDSMLSCIH
     YIIGVTPGDH FDPDIADLEA DIENITRSWP QKLVALVEDS DITQRTSLPT GLTWAGLNWD
     DWAAAFPVGY QERFDLPEAV IDTAYLAGLS PEAPVNVRAY QRLEDLESIF CFKLYTRADR
     AIPLSDILPV LDQMGLKTLE EYGFNVKSWN LGCLWVHEFI IQFAQGARAD FADFAREFQQ
     TILALWYRKT ESDGFNALTI NGASWREIAL LRALCRYRVQ SGLDPSPEVQ QTALRENPDV
     AEALLHLFNL KFSPDLKDIK QREPLVTEAG AQIEALLQKV ASLDHDRVLR RLYLLLNATR
     RTNYFQTDDK GQPKTYISFK VASRELADLP EPKPYREIFV WSPRVEGVHL RFGPVARGGL
     RWSDRKEDFR TEVLGLVKAQ QVKNAVIVPV GSKGGFFPKF LPRPGSSNAT PDTIRNEGIK
     AYKVFLSGLL DLTDNLDAKG KIVPPPQVVA WDDPDPYLVV AADKGTATFS DIANGVAGDY
     GFWLGDAFAS GGSVGYDHKA MGITARGAWE AVKRHFRELG KDIQSEDFTV AGVGDMSGDV
     FGNGMLLSPH IKLVAAFDHR DIFLDPNPDT ARSFAERGRV FALPRSSWQD YDKALISQGG
     GVFSRGQKSI PLSPEVKAML DLTADTVTPF ELMNAILKAR VELLYFGGIG TYVKSPAQSH
     IDVGDKANDA LRIDGSEVRA KVIGEGANLA LTQAGRIACA EAGVRMNTDA IDNSAGVDCS
     DHEVNIKILL GQLTATGRMT LEARNKLLAE MTDEVASHVL KHNYDQTLAL TLQEATAADD
     NANAQAFMTA LEKRGRLDRK VEGLPSNSAL EVRRGQGRGL TRPELAVVMA YGKLVLFDDI
     VASGAPDDAD LEPVLIDYFP DALHGYAADI RKHRLHREII ATVLANDIVN VTGPSFPTRV
     MKGAGVDAEA FVFAFAAARK LFGIQALWAE VSALDAKVPA AAQTGLYRDL SGFIRRQTYW
     IARRFSQTPG PLATRIKPYA DGMAQVLAQG SAVLSETVKA RLEARVTELT GQGAPEDLAR
     RIALLGVFHH VVDVIDLALG PKKPLDKTVE LYFLTGDRFG FDRLTEGAGS LTSADPWDRM
     ATRRLIEDVL IEQKAVVKAM MSRMSPLETP QQIIETWEGE NAGMVQSLQS MIADMQTGGW
     SFAKLTIVNA VLREWVGKL
//