ID A0A1G7GZV5_9RHOB Unreviewed; 555 AA.
AC A0A1G7GZV5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SDE93621.1};
GN ORFNames=SAMN05421538_1166 {ECO:0000313|EMBL:SDE93621.1};
OS Paracoccus isoporae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=591205 {ECO:0000313|EMBL:SDE93621.1, ECO:0000313|Proteomes:UP000199344};
RN [1] {ECO:0000313|EMBL:SDE93621.1, ECO:0000313|Proteomes:UP000199344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22220 {ECO:0000313|EMBL:SDE93621.1,
RC ECO:0000313|Proteomes:UP000199344};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FNAH01000016; SDE93621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7GZV5; -.
DR STRING; 591205.SAMN05421538_1166; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000199344; 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 GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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:UP000199344};
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 191..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 555 AA; 59495 MW; 70872427432EB8D0 CRC64;
MTRHGGQLLV ECLLALGARK GFGVPGESYL AVLDALHDTE GRLDFVLCRN EGGAAFMAAA
WGKLTGQPGL CFVTRGPGVT NASIGIHTAM QDSAPMIIFV GQIGTDMRGR EAFQEIDYRA
VFGTMAKWAV EIDDVDRIPE VLSRAWIAAT TGRPGPVVIA LPEDMLTSLT DKPALTVPPW
IAEPAPAPDA VAEAQRLLTD AKRPLILMGG CNWTHTGRDA LQSFAEASDI PVVAVFRYQD
QFDNHSPVYA GEAGVGMPSH VKALIREADV ILAVNIRFGE MTTDGYTLLD VPVPKQRLIH
VHGSDREIGK IYQPTLGIHA GPNAFAVALS PVSGDRAAWR EKARADWEAS LDVPPQPSPV
DMAAVTKHLR AVLPDDAILT NGAGNFTVWP NKCFPFGPKA RLLAPQSGAM GYGLPAAIAA
QIAHPDRVVV CFAGDGDFHM NFQELGTAMQ AGAQPIVLIL NNGIYGTIRA HQERNYPARV
SGTTLENPDF VALARAFGFH AERIETTDEF APAFARAMRS PNGAVLDLNI SPEALTPRQT
LSQMRDTALA AKDNP
//