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Database: UniProt
Entry: A0A327ZPZ5_9ACTN
LinkDB: A0A327ZPZ5_9ACTN
Original site: A0A327ZPZ5_9ACTN 
ID   A0A327ZPZ5_9ACTN        Unreviewed;       557 AA.
AC   A0A327ZPZ5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Benzoylformate decarboxylase/acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:RAK42838.1};
GN   ORFNames=B0I29_102664 {ECO:0000313|EMBL:RAK42838.1};
OS   Actinoplanes lutulentus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1287878 {ECO:0000313|EMBL:RAK42838.1, ECO:0000313|Proteomes:UP000249341};
RN   [1] {ECO:0000313|EMBL:RAK42838.1, ECO:0000313|Proteomes:UP000249341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7090 {ECO:0000313|EMBL:RAK42838.1,
RC   ECO:0000313|Proteomes:UP000249341};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUN-2018) 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:RAK42838.1}.
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DR   EMBL; QLMJ01000002; RAK42838.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327ZPZ5; -.
DR   OrthoDB; 2443624at2; -.
DR   Proteomes; UP000249341; 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; cd02002; TPP_BFDC; 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:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000249341};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          6..114
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          207..316
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          399..549
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   557 AA;  59002 MW;  327CC1B06D992428 CRC64;
     MTHSTDGGDA VISAFNAVGA DYIFSSPGSE WAPVWESLAR RHRDGLPCPH YLDLLHETVA
     VGMATGYALI TRRAQGVLLH AGPGLLQGSM AVHGALLAGA PMVVTSSESI TYGDGPGPDP
     GGQWYRNLSV VGGPHTLAAP FTKWSNQAAS VHTLTTMITR SAELAARAPA GPVYLNIPLE
     VLLDEWDGPE PKPLAAPGTT VSSAEDIQVV LELLAGAGNP VIVTETTGRE PGGLEALVVF
     AETLGIPVVE PSSAVCVNFP RDHELHAGGD VEPFVDTADV IVLLNCRAPF YPPSRRPATA
     KIVVIDEVPQ RPHIVYQVLN ADHYLEGGVA ATLREMAVRW TEQGLTREAG FAGSEPAAVR
     AAEEKAANNS TGIDPVHLVA TLRDLLGDDS VVVDETITHS RIVQRHLRRT APDSYFYVQG
     GLGQGIAVAL GVKLAAPDKQ VVFTVGDGAF LYNPIVQSLQ AAKANGLPVL ILVFNNTEYR
     SMKMNHLRFY PQGAAVATGE FLGNDLSDQP ELSAFAEPFG MHGEHVTAAE ELVPALDRAL
     KAVRNGTTAI VNVRVSR
//
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