ID A4CC90_9GAMM Unreviewed; 1611 AA.
AC A4CC90;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Putative glutamate dehydrogenase {ECO:0000313|EMBL:EAR27977.1};
GN ORFNames=PTD2_19185 {ECO:0000313|EMBL:EAR27977.1};
OS Pseudoalteromonas tunicata D2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR27977.1, ECO:0000313|Proteomes:UP000006201};
RN [1] {ECO:0000313|EMBL:EAR27977.1, ECO:0000313|Proteomes:UP000006201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D2 {ECO:0000313|EMBL:EAR27977.1,
RC ECO:0000313|Proteomes:UP000006201};
RA Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., Ferriera S.,
RA Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran B.,
RA Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR27977.1}.
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DR EMBL; AAOH01000005; EAR27977.1; -; Genomic_DNA.
DR RefSeq; WP_009839809.1; NZ_CH959301.1.
DR STRING; 87626.PTD2_19185; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_6; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000006201; 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 34..177
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 406..495
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 551..624
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 726..1218
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1263..1601
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1611 AA; 181797 MW; 0A956B6E4DB7D11C CRC64;
MTRNEGHTSV LLDNVCKLIQ KKVHAPNVSL VENFAKTLYS NMSKEDLARR NDSDLYGAVL
SLWNSLEGHT SDDVLIRVFN PELAINGWHS SHTIVEIIAK DMPFLVDSVR MALIRENIAS
HLLLHCPLKI QRNADNTISG ITSLKSEQDS SSTKTVFFIE IDRQTDKKAI ASIAAELESV
LLDVSVAVQD WQAIKGKLIE VTKDIPNRKG KNSADEIQET VEFLDWLARD NFTLMGYRQY
DLLPIQGDYQ LKGVTGSSLG MMKNSVEEKV RLLSDLPEIA RKEAHSDNLL ILTKTNSVSR
VHRPAYIDYI GVKRFDNKGN VIGEDRFIGL FSSNFYNNSA ADVPVLKSKI NRILELSDFA
KGTHAYKAVL NILETYPRDE LLQAKETELL DVAMGVLQVQ ERDMCRLFVR KDVYGRFLSC
MVYVPRERYN TALRRETQQI LGRAFQTSKK VEFTTFFSES ILARTHYTVR LDDNNIEYNV
KDIEHNLIEA ARTWEDKLGS ALIEVAGEAR GNELIRKYAS AFSSSYKEQV LPSAAVVDIE
KLEALNDDNT LEMLFYRPQE ESNSNMVRLS LFHKDVPIHL SDVMPMLENF GLRVIGETPY
AVKTSDGQIN WVMDFSMLLT KNVSDFDKSS VRFQKALTNV WHNRLENDGF NRLVLAGGLT
GREASIMRAY AKYMRQIGVT FSQNYIESTF EHYPDIAIQL VKLFNKKFSP KNKFSEKACE
KLTSEIYTAL DNVANLDDDR IIRSYVDLIT ATIRTNYYQV DAQGDPKSYI SFKVKPNLIP
DMPLPLPAFE IFVYSPRVEG VHLRGGKVAR GGLRWSDRRE DFRTEVLGLV KAQQVKNTVI
VPVGSKGGFV CKQAPSPSDR DAFLKEGQEC YRIFIRGLLD ITDNILAGEI IPPVNVVRHD
EDDPYLVVAA DKGTATFSDI ANSISDEYNF WLGDAFASGG SVGYDHKKMA ITAKGGWESV
KRHFREIGID CQTTDFTCVG IGDMAGDVFG NGMLLSKHIR LQVAFNHMHI FIDPNPDSAT
SWVERERLFN LPRSTWDDYN KDLISEGGGI FLRSAKSITL TPEMKKMLGT KKVAMSPSEL
IKTVLMMPVD LIWNGGIGTY VKAKHETDVG DRANDALRVN GSDINAKIFG EGGNLGCTQL
GRIEFAAKGG RINTDFIDNV GGVACSDNEV NIKILLNSLV AQGDMTRKQR DELLYSMTDE
VSRLVLRDCY RQTHTISVTQ LKGTSTLKEQ IRFIHALEKE GKLDRVIEFL PSDDELAERL
AAGKGLTRPE LSVLVSYAKM VLKEWLVTPE ITDNPYYRQL LVNAFPVPLR DKFNAAMDNH
PLRSEIIATK LANNIINDMG LNFVIRMMEE TGSSAAEVVT CYSMASGVFE MSKTWQEIEA
LDNVIPAIVQ TEMLYQLRRT VRRATRWFLR HRNKALTIEH KLAFYAPAFK DLSENLINYM
SVEESAKLND EAKALEVEGV PVPLAKRIAQ LSSLFSVMDL AQVAKNSERS ISLVADTYFK
LGARMGLHWF LDQITIQPVA NHWQALARAS YREELDWQQR SLAAVVLNSC SKDVCDVDSL
IDSWMTEHEG LLSRWQQMLA EFKTTKVHDF AKFSVALREL MLLSHNCDSS K
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