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
//