ID F6EQ91_HOYSD Unreviewed; 1682 AA.
AC F6EQ91;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=NAD-specific glutamate dehydrogenase {ECO:0000313|EMBL:AEF39514.1};
GN OrderedLocusNames=AS9A_1062 {ECO:0000313|EMBL:AEF39514.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF39514.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF39514.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
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DR EMBL; CP002786; AEF39514.1; -; Genomic_DNA.
DR RefSeq; WP_013805863.1; NC_015564.1.
DR STRING; 443218.AS9A_1062; -.
DR KEGG; asd:AS9A_1062; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_11; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000009235; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT DOMAIN 70..202
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 431..527
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 581..651
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 776..1286
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1333..1668
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1682 AA; 185323 MW; 1A0C61182971E2A3 CRC64;
MTDSHVHSTT GTSAGADAPQ EQPSDADIAS RLEQDSSGDR DLTRLYRTYY RQDAVPSDIG
GAQQPAEGEA ADDHQRRAYR LLQRHRELAA RRTPGTPAVS ISADDARTGN GSGQSNASVL
QIVTDDVPYL VESVTALLGS VGISVEQIVH PVLIVRRDHD GNLAEVLTDR STFDKPDDAL
AESWMHLELT GTPPELTQQI TDRVTKLLGD VRQVVSDTST MRSTLADIAT ELESGRGIGR
AEASEANESA GLLRWLSSGN FRVLGYRRYE VTGRSESGPD LSVVDGSGLG VLRSPEMTDL
RFRLYSDASE AQRLLVFAQG QAPAMSLRVV YPFFVCVRIF NDDDQLIGEH RFLGIFTVTG
LHENVLDVPV LASRVQEVLR MAGHSPDSFS GQSMLEIIQS YPRTELFTAD VQTLYKTVSE
VVAIGVTREL RLFLRADPNG KFVSALVYMP RDRYRTGVRL EMQSILLKEF QGSTIDYTAR
VTESVVAQVH FIIRIPDGWT GGHAPDVSEE ARQRLQTTLG EATRSWEDLL ADEVARQEPT
AHAGRANRHA GAFPQSYKAD FEPVRAISDL KRIDRLEPGG IAIALYRREG AGDGRWQLSL
YLNGESVSLS HVLPVMQSMG VEVLDERPYR LTRSDGAEIW IYDFSLVVDS ETLKTAAVAD
LDGALPTIPE FTDDGVVHND LERRFTEAFA ALWDGLAEAD RFNELILRAG VNWREATMLR
AYARYLRQLG FQYSQSHIED VLLEHSASTS ALVALFEATF DPVNHSRERA EELITQINDH
LDKVVSLDAD RILRAYLRLI RATLRTNYFV AARDDIDPTA GKSRYREVLC FKFDPRDVPE
IPKPRPRFEI FVYSPRIEGV HLRFGEVARG GLRWSDRRED FRTEILGLAK AQAVKNAVIV
PVGAKGGFVV KKPPAVSGDA AADRDAFRAE GIRCYRLFIS GLLDVTDNLD QTSGAVISPA
DVVRQDGDDT YLVVAADKGT ATFSDIANEV AGKYNFWLGD AFASGGSAGY DHKVMGITAR
GAWESVKRHF REEGLDTQSE DFTVVGVGDM SGDVFGNGML LSEHIRLVAA FDHRHVFIDP
NPDAASSFRE RQRMFELPRS SWADYDTSLI SEGGGVWPRS VKSIPISPEI RDVLKLPAGL
DELSPPELIR SILLAPVDLL WNGGIGTYVK SSEETNADCG DKANDAVRVN GSDLRVRVVG
EGGNLGLTQK GRIEFAQRGG KVNSDALDNS AGVDCSDHEV NIKILLESLV SSGDLAPSDR
NGLLASMTDE VAELVLDDNR MQNELMGTSR ANTESLLPVH ARQIADLEAN RGMDREIEAL
PDEGEIDQRI KRGEGLASPE LSTLLAHVKL AIKSDLMDSE LPDHEIFASR LPEYFPEPLR
EQYGSAIKQH PLKREIVTTM IANQTIDNGG ITFTFRLLED AGANTTDSIR AFAAVNTIFG
MTELWTQIRT TDMPTEASDT LILGSRRLLD RASRWLLANR PQPLAVGAEI NRFAATVREL
GPKVPGWLHG NDLRFLKSRT EDAVAQGAPK DLAARVYGLP HEYCLLDIAE VADLSEHEPT
EVAELYYALT AHLGIDMLQG AVSRLERGDR WHALARLALR DDLYGSTRAL CLDVLENAEP
DESAAEKIAE WELSNASRLE RARTALAQIA NSGTLDLATL SVAARQVRSM VHSRSVRSEA
SR
//
