ID A0A0C1JM16_9RHOB Unreviewed; 525 AA.
AC A0A0C1JM16;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetolactate synthase isozyme1 large subunit {ECO:0000313|EMBL:KIC44647.1};
GN ORFNames=RA28_17380 {ECO:0000313|EMBL:KIC44647.1};
OS Ruegeria sp. ANG-S4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC44647.1, ECO:0000313|Proteomes:UP000031326};
RN [1] {ECO:0000313|Proteomes:UP000031326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC44647.1}.
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DR EMBL; JWLK01000005; KIC44647.1; -; Genomic_DNA.
DR RefSeq; WP_039531342.1; NZ_JWLK01000005.1.
DR AlphaFoldDB; A0A0C1JM16; -.
DR STRING; 1577904.RA28_17380; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000031326; 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:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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:UP000031326};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 373..519
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 525 AA; 56500 MW; FF4EFDE3D9028CBC CRC64;
MKRPLGAQIS HALKERGVDV IFGIPGVHNQ EMYRGIEEAG ITHVLARNEQ GAGFMADGYA
RASGKPGVAY VITGPGLCNI MTPMGQAYSD SVPMLVFSSC LDEAQAQRGQ LHQMKDQRAA
ADCVADWSCQ ANTAQAAYGL IERAFEEFEL SRPRTKHIQV PIAQLEAEAD PAPFPNQPAL
HNKCLPPDVA PIMSLLNIAK RPLFILGGGA RSNLWRQILT QLGAACFTTY AGRGMAGVGY
ALDFGAMLPR PSSSEMIASA DLVIAVGTEL AEVDLWRTDL GHSANLIRVD LDPEVLSDRH
RAAVKLQADG ESFARALLAA ADQVQPATGW SPEEVAQARA RWRAEVDAER PGIVPVIDAL
RAAMPVDTMI YSDMTQFAYV AKEIWDMAHP YHWHHPTGFG TLGYAMPAGV GGAVARRGKP
TAVIVGDSGF QYTLPELGTA VELRLPLPII LWDNGKLKEI EDSMVRSQIA PNAVVARNPD
FGKLAEAYGA RSAAPENLDE LQTAVRDAFD APAPTLIRVT PDISG
//