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
//