ID A0A2W7IJP3_9PROT Unreviewed; 577 AA.
AC A0A2W7IJP3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:PZW45932.1};
GN ORFNames=C8P66_110130 {ECO:0000313|EMBL:PZW45932.1};
OS Humitalea rosea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Humitalea.
OX NCBI_TaxID=990373 {ECO:0000313|EMBL:PZW45932.1, ECO:0000313|Proteomes:UP000249688};
RN [1] {ECO:0000313|EMBL:PZW45932.1, ECO:0000313|Proteomes:UP000249688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24525 {ECO:0000313|EMBL:PZW45932.1,
RC ECO:0000313|Proteomes:UP000249688};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
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:PZW45932.1}.
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DR EMBL; QKYU01000010; PZW45932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7IJP3; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000249688; 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:UP000249688};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 10..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 203..336
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 577 AA; 61158 MW; 9468C4A82550A114 CRC64;
MPTANATRTM TGGEAMAEML RLHETGPMFG MGGFQLLPFY DACRRLGLRH YLINDERCGA
FAADAYARVT NRPGVADGTL GPGATNLATG MAEAFNAGMP MICITGDTNR EFSWKNMTQE
ARQLEVLRPL AKEVIRVEVI KRIPELFRRA FAVATSGRPG PVVIDVPEDI AHGSFDFDAD
DFWVDPGTLK AQARRSRPAA EDIARAAALL AHAERPLILA GGGVHISEAY GALLSLAEAE
GIPVAHTMSG KGAIACTHPL SAGVFGRYDR IANAMIAESD CLLVVGCKLG EIATKRFSLF
NGGTPLIHLD VVAEEIGRTT RADVALVGDA RCGLEDLRAA LGGDAAHRAA WTAQVPVRMD
AWRESAREKL EATERPINIG RLMGELNRIL PADAVLVADG GFAGHWGGLL FDTKQAGRGF
VADRGFASIG YGVPGGIGAQ LGVGKTRRVV AMTGDGGFNM SLGDLETARR VGAALVVCVF
NNAASGYVKA LQHAVFGPGA YQSSDLVEMD YAAIAQAMGC KGIRVEDPEQ LADALRAGLA
NTETPTVLDI IVTRDPARML PAADNRTLKV EKGDRPV
//
