ID A0A238JC51_9RHOB Unreviewed; 584 AA.
AC A0A238JC51;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:SMX27737.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:SMX27737.1};
GN Name=ilvB_1 {ECO:0000313|EMBL:SMX27737.1};
GN ORFNames=TRP8649_01847 {ECO:0000313|EMBL:SMX27737.1};
OS Pelagimonas phthalicica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pelagimonas.
OX NCBI_TaxID=1037362 {ECO:0000313|EMBL:SMX27737.1, ECO:0000313|Proteomes:UP000225972};
RN [1] {ECO:0000313|Proteomes:UP000225972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8649 {ECO:0000313|Proteomes:UP000225972};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAY-2017) 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; FXXP01000001; SMX27737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238JC51; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000225972; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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:UP000225972};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:SMX27737.1}.
FT DOMAIN 1..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 401..550
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 584 AA; 63602 MW; 1AF01B4905CA6E4A CRC64;
MKGADILVQM LMGYEVDTVF GVPGDTNVSF YEALQRQEDK ITHIMARDER SAGYMADAYG
RFTKKPGVFE CPSGAGAMYS LPPVAESNAS AVPVILLTID IPLPGEGRGV LTELDCAKLF
EPVTKLSIQV KTAQKLPEII RRAFRVACSG KPGAVHLQIP EDMLTAEVDP ETISLHVEED
CKTFPAFPTR PAPDVLPALL DLIRDAKRPL IVSGGGVNRA CAGVDVQALA ERLNIPVCTT
MTGQGTMPDD HPLAIGVIGD NGYHPHANQS LEEADFVLFV GSRMGSVVTI GWTFPKLTLN
KRVAQIDIDP EVMANNYENL MSVPGDAKLV LQEMLTLVDP AFDTAKHQPW VDHLNALRST
FWDNAQALLN DNNAPLRPER AVRCFNEALE ASGQPALIYS DAGTPTPHMT RFLRLQDCET
RLAIPRAFGG LGSALPATVG AWRADKTKRP IGLFGDGSFG MTTGELETLV RLQVPAILIL
FNNGTFGWIK GLHRLNGHNQ CFGVDFTPPR GQAIAEAFGM KAFTAKSAPE LDTVLQEAFD
YNKGPCFIDV HVESIADRVP PVYSWLRKRG EDPLSLDGKR IGFF
//
