ID H0QTB9_ARTGO Unreviewed; 576 AA.
AC H0QTB9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Putative acetolactate synthase large subunit {ECO:0000313|EMBL:GAB16070.1};
GN ORFNames=ARGLB_110_00310 {ECO:0000313|EMBL:GAB16070.1};
OS Arthrobacter globiformis NBRC 12137.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1077972 {ECO:0000313|EMBL:GAB16070.1, ECO:0000313|Proteomes:UP000003828};
RN [1] {ECO:0000313|EMBL:GAB16070.1, ECO:0000313|Proteomes:UP000003828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12137 {ECO:0000313|EMBL:GAB16070.1,
RC ECO:0000313|Proteomes:UP000003828};
RA Miyazawa S., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Arthrobacter globiformis NBRC 12137.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:GAB16070.1}.
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DR EMBL; BAEG01000110; GAB16070.1; -; Genomic_DNA.
DR RefSeq; WP_003806000.1; NZ_BAEG01000110.1.
DR AlphaFoldDB; H0QTB9; -.
DR STRING; 1077972.ARGLB_110_00310; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000003828; 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; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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:UP000003828};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..331
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..541
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 576 AA; 61201 MW; 3B954FD77F784737 CRC64;
MANQKQVEGG ELVARTLRAA GVEQIFALHG GHLEGFYRAC GAHDLKLVDF RHESSAGHAA
EGYARVTGEL GVCAITAGPG FANAVPAILN AYVDGSPTLF LIGAPPLREK ETNELQGGFD
QMAIAKPMAK WSVSITNVER IPDLLAAAIR HATTGRRGPV VVELPIDVLH MITTEDRVKK
PTGLLVRPRP AAAPRELNEF KDLLLAAKRP AIIVGGDARF SNCEAALLEF ADNSGIPVFS
SKRGLGLLPS GHRSEGHEAS NLAGLSANGS AGPDLVVLAG TRLGLFLGGS GFGVIPEDAK
IVQIYSDAGE IGRIRDVDLA IAADVRTVFE GLNGTIAKDE YPVWDEWRSL AVSLQHHHAA
SYPETENERG IHPFHAAAAL SEVAGPEAVY AIDGGEAGQW AAQQARTSGP GRVITTGYFG
GLGVSPGYAI GAQIAAPERR VAVVTGDGSF GFHLQELDIM VNRNLPIVTL ILNNEVWGMS
IHGQQIMYGK DYSAISELPG RNYAAIARAF GCHAERVTSF DDLKPALERA FEAGIPAVVE
VMTDPEVVSP GLINMLGTVE DESQQIMVPY YENIPR
//
