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Database: UniProt
Entry: A4XF89_NOVAD
LinkDB: A4XF89_NOVAD
Original site: A4XF89_NOVAD 
ID   A4XF89_NOVAD            Unreviewed;       315 AA.
AC   A4XF89;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Dehydrogenase, E1 component {ECO:0000313|EMBL:ABP64600.1};
GN   OrderedLocusNames=Saro_3741 {ECO:0000313|EMBL:ABP64600.1};
OS   Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS   56034 / CIP 105152 / NBRC 16084 / F199).
OG   Plasmid pNL2 {ECO:0000313|EMBL:ABP64600.1,
OG   ECO:0000313|Proteomes:UP000009134}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238 {ECO:0000313|EMBL:ABP64600.1, ECO:0000313|Proteomes:UP000009134};
RN   [1] {ECO:0000313|EMBL:ABP64600.1, ECO:0000313|Proteomes:UP000009134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC   / F199 {ECO:0000313|Proteomes:UP000009134};
RC   PLASMID=pNL2 {ECO:0000313|EMBL:ABP64600.1,
RC   ECO:0000313|Proteomes:UP000009134};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Han C., Thomson S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Fredrickson J., Romine M.F., Richardson P.;
RT   "Complete sequence of plasmid pNL2 of Novosphingobium aromaticivorans DSM
RT   12444.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP000677; ABP64600.1; -; Genomic_DNA.
DR   RefSeq; WP_011906983.1; NC_009427.1.
DR   AlphaFoldDB; A4XF89; -.
DR   KEGG; nar:Saro_3741; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_5_0_5; -.
DR   Proteomes; UP000009134; Plasmid pNL2.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Plasmid {ECO:0000313|EMBL:ABP64600.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009134}.
FT   DOMAIN          19..304
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   315 AA;  33501 MW;  602FD27DD9BAC0D6 CRC64;
     MSGPDPALLE SMFHKLAVSR AVETLMLRHT REERFSGWWH PGEGQEAAPI GATAALEADD
     YVWYQGRGCA WAIGKGMDPL PILGDLLGKT NGATGGKGGG VPHWADYSLG IMGEGATLGS
     VYPLAAGSAL ASKIRKDGRV SLANFGDGTA SRGTFHETMM HAAAWKLPLI YFCENNGLLV
     GTRTEQVSAT ADIANLAKGY GIPGVIVDGQ DAVAVWEATR EAAARARAGK GPTLIEAKVT
     RKHGHYAGDP QHYRDPDYLR DYRDPLDLLA ARLAGNVAAR IVEQADAEVA AAYEAARAAP
     EPDVSVIERD LYHVV
//
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