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Database: UniProt
Entry: K6DQX4_9BACI
LinkDB: K6DQX4_9BACI
Original site: K6DQX4_9BACI 
ID   K6DQX4_9BACI            Unreviewed;       320 AA.
AC   K6DQX4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=HMGL-like family protein {ECO:0000313|EMBL:EKN70603.1};
GN   ORFNames=BABA_04149 {ECO:0000313|EMBL:EKN70603.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN70603.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN70603.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+);
CC         Xref=Rhea:RHEA:19045, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30934, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.3.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00034270};
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:EKN70603.1}.
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DR   EMBL; AJLS01000036; EKN70603.1; -; Genomic_DNA.
DR   RefSeq; WP_007083865.1; NZ_AJLS01000036.1.
DR   AlphaFoldDB; K6DQX4; -.
DR   STRING; 1117379.BABA_04149; -.
DR   PATRIC; fig|1117379.3.peg.857; -.
DR   eggNOG; COG0119; Bacteria.
DR   OrthoDB; 9804858at2; -.
DR   Proteomes; UP000006316; Unassembled WGS sequence.
DR   GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd07944; DRE_TIM_HOA_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005675; Citramal_synthase.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR43538:SF1; (R)-CITRAMALATE SYNTHASE; 1.
DR   PANTHER; PTHR43538; ALPHA-IPM SYNTHASE/HOMOCITRATE SYNTHASE; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT   DOMAIN          5..257
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   320 AA;  36583 MW;  5267257E9F9E61C6 CRC64;
     MEQRCKILDC TIRDGGLVNN WDFSIEFVQD LYNGLSAAGV EYMEIGYKNS PKLLNATEPN
     PWRFLDDNFL KEIIPEKKFT KLSALVDIGR VDPNDILPRE ESVLDMIRVA CYIREVDKGL
     ELVQMFHDLG YETSLNIMAL SSVPEKKLIE AFELVRNSPV DVVYIVDSFG SLDPADIEHQ
     VKKFKEMIPN KQLGIHTHNN MQLAFANTLS AMKNGVTFLD SSVYGMGRAA GNCHTELLVS
     YVPKTSYELK PVLGIIEKHM LEMRQKWEWG YIIPYMISGV LNEHPRVAMA YRESDDRDKF
     LDFYDKVTSP EVALASVRNR
//
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