(data stored in SCRATCH zone)

SWISSPROT: Q13SG3_PARXL

ID   Q13SG3_PARXL            Unreviewed;       399 AA.
AC   Q13SG3;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 92.
DE   RecName: Full=2-amino-3-ketobutyrate coenzyme A ligase {ECO:0000256|HAMAP-Rule:MF_00985};
DE            Short=AKB ligase {ECO:0000256|HAMAP-Rule:MF_00985};
DE            EC=2.3.1.29 {ECO:0000256|HAMAP-Rule:MF_00985};
DE   AltName: Full=Glycine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_00985};
GN   Name=kbl {ECO:0000256|HAMAP-Rule:MF_00985};
GN   ORFNames=Bxe_B3021 {ECO:0000313|EMBL:ABE32976.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE32976.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE32976.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE32976.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the cleavage of 2-amino-3-ketobutyrate to
CC       glycine and acetyl-CoA. {ECO:0000256|HAMAP-Rule:MF_00985}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA;
CC         Xref=Rhea:RHEA:20736, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:78948; EC=2.3.1.29;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00985};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00985};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00985};
CC   -!- PATHWAY: Amino-acid degradation; L-threonine degradation via
CC       oxydo-reductase pathway; glycine from L-threonine: step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00985}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00985}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|HAMAP-Rule:MF_00985}.
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DR   EMBL; CP000271; ABE32976.1; -; Genomic_DNA.
DR   RefSeq; WP_011490365.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_B3021; -.
DR   EnsemblBacteria; ABE32976; ABE32976; Bxe_B3021.
DR   GeneID; 4006477; -.
DR   KEGG; bxb:DR64_5350; -.
DR   KEGG; bxe:Bxe_B3021; -.
DR   PATRIC; fig|266265.5.peg.4668; -.
DR   eggNOG; ENOG4107EEK; Bacteria.
DR   eggNOG; COG0156; LUCA.
DR   HOGENOM; HOG000221022; -.
DR   KO; K00639; -.
DR   OMA; MDTHGFG; -.
DR   OrthoDB; 479874at2; -.
DR   BioCyc; BXEN266265:BXE_RS22125-MONOMER; -.
DR   UniPathway; UPA00046; UER00506.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00985; 2am3keto_CoA_ligase; 1.
DR   InterPro; IPR011282; 2am3keto_CoA_ligase.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01822; 2am3keto_CoA; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13SG3.
DR   SWISS-2DPAGE; Q13SG3.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00985,
KW   ECO:0000313|EMBL:ABE32976.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Ligase {ECO:0000313|EMBL:ABE32976.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00985,
KW   ECO:0000256|SAAS:SAAS00473492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00985,
KW   ECO:0000313|EMBL:ABE32976.1}.
FT   DOMAIN       44    389       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
FT   REGION      111    112       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00985}.
FT   REGION      210    213       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00985}.
FT   REGION      241    244       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00985}.
FT   REGION      274    275       Pyridoxal phosphate binding; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00985}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00985}.
FT   BINDING     185    185       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00985}.
FT   BINDING     370    370       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00985}.
FT   MOD_RES     244    244       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00985}.
SQ   SEQUENCE   399 AA;  42836 MW;  2ADEC6B78C773190 CRC64;
     MRDLYLAHLR DTLEQIRADG FYKNERVIAS PQSADIRLAD GAAVLNFCAN NYLGLADDAR
     LIDAAKQGLD SDGFGMASVR FICGTQTVHK ELEQALAAFL QTDDCILYSS CFDANGGLFE
     TLLDENDAII SDELNHASII DGVRLSKAKR SRYKNNDLAD LEARLIEAQA AGARFKLIAT
     DGVFSMDGII ADLAGICDLA DRYGALVMVD DSHAVGFVGE HGRGTPEHCG VLSRVDIITG
     TLGKALGGAS GGYVAARKEI VELLRQRSRP YLFSNTLTPS IAAASLKVLE LLASEEGAQL
     RARVRENGAH FRSKMSALGF TLVPGEHPII PVMLGDAQLA SKMADALLKE GVYVIGFSFP
     VVPKGRARIR TQMSAAHTPG QIDRAVDAFA RVGRELGVI
//

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