ID Q1YPM0_9GAMM Unreviewed; 1646 AA.
AC Q1YPM0;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAS46151.1};
GN ORFNames=GB2207_00775 {ECO:0000313|EMBL:EAS46151.1};
OS gamma proteobacterium HTCC2207.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Porticoccaceae; SAR92 clade.
OX NCBI_TaxID=314287 {ECO:0000313|EMBL:EAS46151.1, ECO:0000313|Proteomes:UP000005555};
RN [1] {ECO:0000313|EMBL:EAS46151.1, ECO:0000313|Proteomes:UP000005555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2207 {ECO:0000313|EMBL:EAS46151.1,
RC ECO:0000313|Proteomes:UP000005555};
RA Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (MAR-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:EAS46151.1}.
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DR EMBL; AAPI01000009; EAS46151.1; -; Genomic_DNA.
DR STRING; 314287.GB2207_00775; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_6; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000005555; 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; 2.
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..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 583..661
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 761..1255
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1305..1635
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 1646 AA; 186764 MW; 91E868D2B1FE45AE CRC64;
MDAKNINQRG ELITSLNKIA TRQLTQFQAQ QFDNFIANAM HFYPDADYLA RPAQDIFWNL
WGLCRFSAES VEATNAENRA RVRVFNPDPE LDGWSSAHTT IYINQRDMPF LVDSLRIVLN
RRGLNVFTLQ SNPVWVVRNP QGAVERTHAD FAEGAEREAL ITVEVDLHAE SEFVDLRREL
LDVLNDVEVV VAEFDPMRQR VETLIEELQN NAPEVEQLAE SLEFLRWIHN GYFTFTGCVE
FDLKVDGDKL YLSEAADSRC GLLKKYSGDR REGWVEELSP GVRALYESDE LLTITKSSQR
SRVHRDVYSD YVVVKRFDTL GLPCGEVRFM GLYTSQFYSY SPRRIPVLRN KVNWVLENSG
FKASSHDGKA LMAILDFHPR DELFFVSRED LAEIAIGIWQ IYERRVIKAF IHPDPFDKFV
SCIVYLPRES FSTQARMKIQ HSIGDRLDAV ESEFTTQFLP ESVLVRIYLV YQVRNKSYLN
VDGADLEDIV RQVTRDWCDE FAALAIEQGF EAQSTEIKST DIQSTYIKST DIKSTDTKST
VAQGAALARR FQRAFPAAYR ELYSPHQALA HIALFESLEG AADIAIELQH QQAAENNHLQ
LKLFHRHQPL ELSDMIPMLE NLGFRVVMEH PYLIRPEADG DVWLQEFQLS FSLDVNVDVE
AVQGSFKEAL STVWKGDAEN DSFNRLVIGA RLDWRAVAML RLYARYLKQL GISYSQEFIA
DTLSRYLDIT RNLVALFKSY FDPRYAGESR GERFQGLASK ILGALDDVDN ISEDNVIRSY
LEVIQATLRT NFFQTIEDGS YKSYISVKLE SGKISLAPKP RPEFEIFVYS PRVEGVHLRG
GKVARGGLRW SDRLEDYRTE VLGLVKAQQV KNAVIVPTGA KGGFVAKQAS MDAGRDAWLQ
EGIASYMLYI QALLDITDNI IEGEIVPPAD VIRRDGDDPY LVVAADKGTA TFSDIANEIS
HANNFWLGDA FASGGGNGYD HKAMGITARG AWVAVQRHFR EIGIDIQQQD FTVVGVGDMG
GDVFGNGMLL SEHIQLVSAF NHLHIFVDPN PDAASTFVER QRLFDTPRST WDDFDRSLMS
EGSAIYSRSS KSLTLTPQIK ERFAIENDEV TPTELINGML KSPVDLIWNG GIGTYVKASS
ENNADVGDRA NDVLRVDGRD LRCKVFGEGG NLGMTQRGRI EFCLKGGLCN TDFIDNAAGV
DCSDHEVNIK ILLNQLVLNG QLGVEERNDF LESMTDTVAE LVLHNNLRQT QAISLAQHRS
DQQHAEYQRF MAWLESSGKL DRELEFLPTD DQLSERINRH KPSWTRPELA VLVCYSKVML
KEALVAADLL SEPYLAASVE RAFPSALVER YPDEVIGHQL RQEIVATQLA NDMVDRVGFS
FFFRQMESTG ASVGDVIRAY STAMNILGLH QLWDSIEGSD LPATVQLDLL HIVIRLTRRT
TRWLLRNRRQ TLNCSEIINQ FTGPMDLVLQ QLEELHEVEW INLWSAEKDN ITELGVEDKL
ASRLAASDSM FISLGVVDTV LELDKPVQQV AKLYFRLGEF LSLDWFMAQI VALHPENRWE
DLARESYVDD LEGQRRRLTA NLLRDIEGDN LDLLVEDWQQ QQAPLIDRWR FMIKDLRHGP
TPDFAMISVA LRELLDLVQA SIDGRE
//
