ID A0A249T143_9BACT Unreviewed; 268 AA.
AC A0A249T143;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=Alpha-acetolactate decarboxylase {ECO:0000256|ARBA:ARBA00020164, ECO:0000256|PIRNR:PIRNR001332};
DE EC=4.1.1.5 {ECO:0000256|ARBA:ARBA00013204, ECO:0000256|PIRNR:PIRNR001332};
GN ORFNames=CK934_22950 {ECO:0000313|EMBL:ASZ13603.1};
OS Chitinophaga sp. MD30.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2033437 {ECO:0000313|EMBL:ASZ13603.1, ECO:0000313|Proteomes:UP000217148};
RN [1] {ECO:0000313|EMBL:ASZ13603.1, ECO:0000313|Proteomes:UP000217148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD30 {ECO:0000313|EMBL:ASZ13603.1,
RC ECO:0000313|Proteomes:UP000217148};
RA Wan X., Darris M., Hou S., Donachie S.P.;
RT "Draft genome sequence of a novel Chitinophaga sp., MD30, isolated from a
RT biofilm in an air conditioner condensate pipe.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-acetolactate + H(+) = (R)-acetoin + CO2;
CC Xref=Rhea:RHEA:21580, ChEBI:CHEBI:15378, ChEBI:CHEBI:15686,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=4.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001784,
CC ECO:0000256|PIRNR:PIRNR001332};
CC -!- PATHWAY: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-
CC butane-2,3-diol from pyruvate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00005170, ECO:0000256|PIRNR:PIRNR001332}.
CC -!- SIMILARITY: Belongs to the alpha-acetolactate decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00007106, ECO:0000256|PIRNR:PIRNR001332}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP023254; ASZ13603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249T143; -.
DR OrthoDB; 8612680at2; -.
DR UniPathway; UPA00626; UER00678.
DR Proteomes; UP000217148; Chromosome.
DR GO; GO:0047605; F:acetolactate decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045151; P:acetoin biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd17299; acetolactate_decarboxylase; 1.
DR InterPro; IPR005128; Acetolactate_a_deCO2ase.
DR PANTHER; PTHR35524; ALPHA-ACETOLACTATE DECARBOXYLASE; 1.
DR PANTHER; PTHR35524:SF1; ALPHA-ACETOLACTATE DECARBOXYLASE; 1.
DR Pfam; PF03306; AAL_decarboxy; 1.
DR PIRSF; PIRSF001332; Acetolac_decarb; 1.
DR SUPFAM; SSF117856; AF0104/ALDC/Ptd012-like; 1.
PE 3: Inferred from homology;
KW Acetoin biosynthesis {ECO:0000256|ARBA:ARBA00023061,
KW ECO:0000256|PIRNR:PIRNR001332};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW ECO:0000256|PIRNR:PIRNR001332};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001332};
KW Reference proteome {ECO:0000313|Proteomes:UP000217148}.
SQ SEQUENCE 268 AA; 29560 MW; B91BA855AD7E5CBE CRC64;
MNYKLLLTIL IVPTALFAQV TKKQPAPGNK SRTLLTAGIA GGLIGGLYDG LYPVSILKAN
GDFGLGAPDK IDGELVMFKG KVYQTQASGQ TFEVTNDPLI PFAMVNYFHA DHSVKIPAGM
NKPAFFHCLD SLLTNPNGLY AIHIKGRFAK MRTRAFPPSE PPYPALSAIL DKQHFFEYTA
TSGDLIGYRL PAFMDNTNIS GYHFHYLSDS KKQGGHMVDL YTDDITVEIS ELDSYTVLVP
TKNAAFDHFD FKKDRGEDIK SVERGAKK
//
