ID K6X897_9MICO Unreviewed; 542 AA.
AC K6X897;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative acetolactate synthase large subunit {ECO:0000313|EMBL:GAB95049.1};
GN ORFNames=KILIM_015_01110 {ECO:0000313|EMBL:GAB95049.1};
OS Kineosphaera limosa NBRC 100340.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Kineosphaera.
OX NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB95049.1, ECO:0000313|Proteomes:UP000008366};
RN [1] {ECO:0000313|EMBL:GAB95049.1, ECO:0000313|Proteomes:UP000008366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB95049.1,
RC ECO:0000313|Proteomes:UP000008366};
RA Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL Submitted (AUG-2012) 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:GAB95049.1}.
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DR EMBL; BAHD01000015; GAB95049.1; -; Genomic_DNA.
DR RefSeq; WP_006591581.1; NZ_BAHD01000015.1.
DR AlphaFoldDB; K6X897; -.
DR STRING; 1184609.KILIM_015_01110; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000008366; 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:UP000008366};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..528
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 542 AA; 56464 MW; 00B59067C9687B3C CRC64;
MARNGGDLVV ETLTALGAGT VFGIPGQHAL GLFDALSRSE LSFVSSRVEN NAAFAADGFA
RATGKVAVLF LSTGPGALTA LAGLEEAYAT GVPIVVVSSQ IPRAGLGGRR KGMLHQLDEQ
RAAAAQVTKW QRTVFDASSI APAIADAWAQ AVTAPAGPVW VEVPQDVLLE EVEVPASTPA
LVARPVEPAP ELVAEAARLL TGADRVAIVA GGGVRRAGAE AALIGVAEAL GAPVACSPGG
HGAFPWTHPL SLQSWVEDRH VTRVLEEADV LLVLGSALGQ VTSNYFTLAP RGRVVQVDAD
ERVLGSNHTV LGIRADAGEF LRALASLLPS DRPNSAGQAL AAQTLAQVEA RLDAQDLRHE
RAFLDRIRAA VPDDMQTFWD MTIAAYWAWS CWDSRGGEFH SGQGAGGLGF AYPAAIGGSL
GLRDQGRPER VLAVAGDGSA MYSIAELATA RQHDAAVTWL IVDDGGYGIL REYMQDAFGA
ATHTELTRPD FAALAATFGI PAVTVAPEDV EEALRDALAA TGPNVVVVPT LLRMFAPTHL
DA
//
