ID U2YA56_9SPHN Unreviewed; 537 AA.
AC U2YA56;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative acetolactate synthase large subunit {ECO:0000313|EMBL:GAD50246.1};
GN ORFNames=NT2_08_00330 {ECO:0000313|EMBL:GAD50246.1};
OS Caenibius tardaugens NBRC 16725.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Caenibius.
OX NCBI_TaxID=1219035 {ECO:0000313|EMBL:GAD50246.1, ECO:0000313|Proteomes:UP000016568};
RN [1] {ECO:0000313|EMBL:GAD50246.1, ECO:0000313|Proteomes:UP000016568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16725 {ECO:0000313|EMBL:GAD50246.1,
RC ECO:0000313|Proteomes:UP000016568};
RA Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Novosphingobium tardaugens NBRC 16725.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:GAD50246.1}.
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DR EMBL; BASZ01000008; GAD50246.1; -; Genomic_DNA.
DR RefSeq; WP_021691064.1; NZ_CP034179.1.
DR AlphaFoldDB; U2YA56; -.
DR KEGG; ntd:EGO55_03075; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000016568; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000016568};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 396..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 537 AA; 56812 MW; B18217C3FAF8C2B2 CRC64;
MPEMMTGGQA ITAALEALGV TCVFGVPSQQ NLALYEALSH SQTIRVVGAR NEAGAAHAAD
GYARATGKLG VAITSTGPGT TNAVTGLYEA GFASSPVLLI TTQIDRVHLG RNRGFIHEAE
GQLPMLQAVT RRAERPLHGH QLYDTILRMG RDIQSGRPQP GAIEVPTDML GEMTAVERTP
FTKAPPHVPG ADAIAHVADL LNGASRPLLW LGGGCVRSGD AEAIRAFVDH FGAPVITTPN
GRSALSTDHP LALGSAPHYP AFRALLDQAD VVLAVGTRFQ FVTSAYWTLP LGKNLIQIDV
DGSMIGRNYP AAASLIGDAA ATLNALRQTL PQQQPDPQFL ALAQETRRAI DADSAQRAGP
DHAQLCAIID EVLPHDRNIV CDATMVGNTW ATYRLPVRDF QGFTYSTSLA IGPALPLAIG
AAVGSNRRTI AIHGDGGVML NIGEMATAVE TRAPLTLLVF NDHGYGILKT LQKQTGLTPF
ACDLHTPDFV GIGRAMGMAA ERVTSPDEFR TAFERSVATE GPSLIEIDLT QIQALSL
//
