(data stored in ACNUC7421 zone)

SWISSPROT: C5BB98_EDWI9

ID   C5BB98_EDWI9            Unreviewed;       398 AA.
AC   C5BB98;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
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   OrderedLocusNames=NT01EI_0073 {ECO:0000313|EMBL:ACR67333.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67333.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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: Acetyl-CoA + glycine = CoA + 2-amino-3-
CC       oxobutanoate. {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; CP001600; ACR67333.1; -; Genomic_DNA.
DR   RefSeq; WP_015869554.1; NC_012779.2.
DR   ProteinModelPortal; C5BB98; -.
DR   STRING; 634503.NT01EI_0073; -.
DR   EnsemblBacteria; ACR67333; ACR67333; NT01EI_0073.
DR   GeneID; 7959792; -.
DR   KEGG; eic:NT01EI_0073; -.
DR   PATRIC; fig|634503.3.peg.66; -.
DR   eggNOG; ENOG4107EEK; Bacteria.
DR   eggNOG; COG0156; LUCA.
DR   HOGENOM; HOG000221022; -.
DR   KO; K00639; -.
DR   OMA; MDTHGFG; -.
DR   OrthoDB; POG091H024U; -.
DR   UniPathway; UPA00046; UER00506.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
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; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR13693:SF65; PTHR13693:SF65; 1.
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; C5BB98.
DR   SWISS-2DPAGE; C5BB98.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00985,
KW   ECO:0000313|EMBL:ACR67333.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Ligase {ECO:0000313|EMBL:ACR67333.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00985,
KW   ECO:0000256|SAAS:SAAS00655949};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00985,
KW   ECO:0000313|EMBL:ACR67333.1}.
FT   DOMAIN       43    386       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     368    368       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   398 AA;  42775 MW;  F43FC4C91E528335 CRC64;
     MSADFYQQLA QQLVATRAEG LYKTERIITS AQQAEIAVAD GSRVLNFCAN NYLGLADHPA
     LIAAAKEGME SHGFGMASVR FICGTQDSHK ALEQQLAAFL GMEDAILYSS CFDANGGLFE
     TLLGPEDAII SDALNHASII DGVRLCKARR YRYANNDMAE LKARLELARA EGARHIMIAT
     DGVFSMDGVI ADLRSICDLA DEYDALVMVD DSHAVGFVGG HGRGTPEYCG VVGRVDIMTG
     TLGKALGGAS GGYTAARKEV VEWLRQRSRP YLFSNSLAPA IVAASSRVLT LLAQGDDLRA
     RLWDNARLFR EKMTAAGFTL AGADHAIIPV MLGEAKLAQH FADLLLQEGI YVTGFFYPVV
     PQGQARIRTQ MSAAHTPAQI EQAVAAFIRV GKQLGVIA
//

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