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Database: UniProt
Entry: A0A0D8PRL3_9GAMM
LinkDB: A0A0D8PRL3_9GAMM
Original site: A0A0D8PRL3_9GAMM 
ID   A0A0D8PRL3_9GAMM        Unreviewed;       554 AA.
AC   A0A0D8PRL3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Acetolactate synthase AlsS {ECO:0000313|EMBL:PSV89578.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:PSV89578.1};
GN   ORFNames=C9I88_18780 {ECO:0000313|EMBL:PSV89578.1};
OS   Photobacterium iliopiscarium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=56192 {ECO:0000313|EMBL:PSV89578.1, ECO:0000313|Proteomes:UP000241954};
RN   [1] {ECO:0000313|EMBL:PSV89578.1, ECO:0000313|Proteomes:UP000241954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 13481 {ECO:0000313|EMBL:PSV89578.1,
RC   ECO:0000313|Proteomes:UP000241954};
RA   Butler K.;
RT   "Whole genome sequencing of Histamine producing bacteria.";
RL   Submitted (JAN-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:PSV89578.1}.
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DR   EMBL; PYLW01000033; PSV89578.1; -; Genomic_DNA.
DR   RefSeq; WP_045038425.1; NZ_PYOP01000025.1.
DR   AlphaFoldDB; A0A0D8PRL3; -.
DR   GeneID; 70040756; -.
DR   OrthoDB; 9785953at2; -.
DR   Proteomes; UP000241954; 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   GO; GO:0034077; P:butanediol metabolic process; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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; IPR012782; Acetolactate_synth_catblc.
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; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR02418; acolac_catab; 1.
DR   PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:PSV89578.1}.
FT   DOMAIN          7..120
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          192..324
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          388..534
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   554 AA;  60156 MW;  30B43E8472DCC905 CRC64;
     MLNKTISGAE LVVKTLKAHD VPHIFGIPGA KIDSVFDAVC DDGPEIIICH HEQNAAFMAA
     ATGRLTGKAG VCLATSGPGA SNLVTGVATA NSEGDPVVAL AGAVPLSMYS HNTHQSMDTR
     SLFNPITKFS AEVMDSASLP DVVHKAFRIS EQPTQGASFV SLPQDVLTNQ IPFIPVQQPK
     PILFGGAHPQ AIRQAADLIN AAKNPVLLLG MDASQPFVTG AIRQLLEQTK IAVVNTFAAA
     GVISHNLYDC FLGRVGLFKN QPGDIALNNA DLIITIGYSP IEYDPILWNK DGKTPIIHVG
     YQQADLEASY NPISEVVGDV AVSVASIAAE LDQRESLENN QKFQDLRQDL QQIMRMGVNK
     TSSMGVHPLR FVHDLRRFVS DDTTVCCDVG SIYIWMARYF HSFEPRRLLF SNGQQTLGVA
     LPWAIAASLL TPNEKVISMS GDGGFLFSSM ELATAVRHKC NIVHFVWTDH SYDMVKIQQL
     KKYGRESAVS FMGPDIVKYA ESFGAYGLAI NTADDIEPVL RKAMALSGPV LVNVNIDYRD
     NSRLLDQLHP CQQD
//
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