ID W2UF70_9GAMM Unreviewed; 1621 AA.
AC W2UF70;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:ETN92584.1};
DE EC=1.4.1.2 {ECO:0000313|EMBL:ETN92584.1};
GN Name=gdhB {ECO:0000313|EMBL:ETN92584.1};
GN ORFNames=U062_00460 {ECO:0000313|EMBL:ETN92584.1};
OS Gammaproteobacteria bacterium MOLA455.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Porticoccaceae.
OX NCBI_TaxID=1411685 {ECO:0000313|EMBL:ETN92584.1, ECO:0000313|Proteomes:UP000018839};
RN [1] {ECO:0000313|EMBL:ETN92584.1, ECO:0000313|Proteomes:UP000018839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOLA455 {ECO:0000313|EMBL:ETN92584.1,
RC ECO:0000313|Proteomes:UP000018839};
RX PubMed=24482511;
RA Courties A., Riedel T., Jarek M., Papadatou M., Intertaglia L., Lebaron P.,
RA Suzuki M.T.;
RT "Draft Genome Sequence of the Gammaproteobacterial Strain MOLA455, a
RT Representative of a Ubiquitous Proteorhodopsin-Producing Group in the
RT Ocean.";
RL Genome Announc. 2:e01203-e01213(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:ETN92584.1}.
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DR EMBL; AZIN01000001; ETN92584.1; -; Genomic_DNA.
DR STRING; 1411685.U062_00460; -.
DR PATRIC; fig|1411685.3.peg.447; -.
DR eggNOG; COG2902; Bacteria.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000018839; 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,
KW ECO:0000313|EMBL:ETN92584.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018839}.
FT DOMAIN 35..180
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 408..497
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 558..636
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 736..1230
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1280..1610
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
FT COILED 198..225
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1621 AA; 183964 MW; 240A575A81BB848A CRC64;
MDAKTYNQRG VLIASLNKIA ARQLTQSHAQ QFDGFIANAM HFYPDADYLA RPIQDIFWNL
WGLCRFSAEQ IDMASTESRA RVRVFNPDPE LDGWLSGHTT IYINQRDMPF LVDSLRNVLN
RRGLNIFTLQ SNPVWVVRNA QGVVERTCAD FAENAEREAL ITIEVDLHLE SELSDLRREL
LDVLDDVEVV VADFDPMRQR VETLIEELQN NAPEVEQLNE SLEFLRWIQN GYFTFTGCVE
FDLKIDGDNL YLSEAADSRC GLLRKYSGDR REGWVEELSP GVRALYESDE LLTITKSSQR
SRVHRDVYSD YVVVKRFDRD GQPCGEVRFM GLYTSQFYSY SPRRIPILRN KVNWVMENSG
FKATSHDGKA LMAILDFHPR DELFFLSRES LAETAIGIWQ IYERRVIKAF VHPDPFDKFV
SCIVYLPRES FSTQARMKIQ HSIGDRLDAV ESEFTTQFLP ESVLVRIYLV YQVRNKQYLN
VVSSDLEDIV RQVTRDWCDE FAAVVIEQGA ENRSTETQSA TLTRRFQRAF PGAYRELYSP
LQALAHIELF DILEGTGDIA IQLQHQLAVE NNHLQLKLFH RQTPLELSDM IPMLENLGFR
VVMEHPYLIR PEGDADVWMQ EFQLSFSLDV NVDVEAVQGS FKEALSTVWK GDAENDSFNR
LVIGARLDWR AVAMLRLYAR YLKQLGISYS QEFIADTLCR YLEITRNLVA LFKSYFDPRY
AGETRSERVQ GLVIKILSAL DDVDNISEDN VIRSYLEVIQ ATLRTNFFQT IEDGSCKSYI
SVKLESGKIS LAPKPRPEFE IFVYSPRVEG VHLRGGKVAR GGLRWSDRLE DYRTEVLGLV
KAQQVKNAVI VPTGAKGGFV AKQASLAAGR DAWLQEGIAS YMLYIQALLD ITDNIIEGKI
VPPVDVVRRD GDDPYLVVAA DKGTATFSDI ANEISHANNF WLGDAFASGG GNGYDHKAMG
ITARGAWVAV QRHFREIGID IQQQDFTVIG VGDMGGDVFG NGMLLSEHIR LVSAFNHLHI
FVDPNPDAAS TFVERQRLFD TPRSSWDDFD RGLMSEGSAI YSRDSKSLTI TPQIKQRFAI
EQDEMTPTEL INAILKSPVD LIWNGGIGTY VKASSENNAE VGDRANDALR VNGRDLRCKV
FGEGGNLGMT QRGRIEFCLK GGLCNTDFID NAAGVDCSDH EVNIKILLNQ LLLNGHLGVA
ERNQFLESMT DTVAELVLHN NLRQTQAISL AQHRSDLQHA EYQRFMAWLE SSGKLDRELE
FLPTDDQLGE RINRHKPSWT RPELAVLVCY SKVMLKEALV VADLLSEPFL AASVERAFPP
ALVARYPDEV ANHQLRQEIV ATQLANDMVD RVGFSFFFRQ MESTGASAGD VIRAYSIAMN
ILGLHQLWDN IENSDLPATV QLDLLHILIR LTRRTTRWLL RNRRHNLNCS EIVGQFTAPM
HLLLQQLPEL HEVEWIKLWS AEKANITELG VDDLLASRLA ASDSMFICLG VVDTALYLGK
PVQQVAKLYF KLGEFLSLDW FMAQIVALNP GNRWQDLARE SYVDDLEGQR RRLTANLMGD
LVGDNIQLLV EGWQQQQAPL IERWRFMIKD LRHGPTPDFA MISVALRELL DLVQASIDGR
G
//
