(data stored in SCRATCH zone)

SWISSPROT: A8FPE1_SHESH

ID   A8FPE1_SHESH            Unreviewed;       397 AA.
AC   A8FPE1;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 72.
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=Ssed_0101 {ECO:0000313|EMBL:ABV34714.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34714.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34714.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34714.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV34714.1; -; Genomic_DNA.
DR   RefSeq; WP_012004240.1; NC_009831.1.
DR   ProteinModelPortal; A8FPE1; -.
DR   STRING; 425104.Ssed_0101; -.
DR   EnsemblBacteria; ABV34714; ABV34714; Ssed_0101.
DR   KEGG; sse:Ssed_0101; -.
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; UP000002015; Chromosome.
DR   GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:UniProtKB-HAMAP.
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; -; 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; 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; A8FPE1.
DR   SWISS-2DPAGE; A8FPE1.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00985,
KW   ECO:0000313|EMBL:ABV34714.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00985,
KW   ECO:0000256|SAAS:SAAS00655949};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00985,
KW   ECO:0000313|EMBL:ABV34714.1}.
FT   DOMAIN       42    387       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   397 AA;  43138 MW;  C5F9B19E35B588C9 CRC64;
     MTTTSFYNQI NQQLADVKAE GLYKSERVIV SPQQTEIRVN GTEVMNFCAN NYLGLANHPE
     LIKAAQAGLN DHGFGMASVR FICGTQDIHK QLESSLSEFL GMEDTILYSS CFDANAGLFE
     TLLSAEDAII SDALNHASII DGVRLCKAKR FRYANNDMAD LEAQLKAAKE AGARNIMIAT
     DGVFSMDGVI ANLKGVCDLA DKYGALVMVD DSHAVGFIGA NGRGTHEYCE VMDRVDIITG
     TLGKALGGAS GGFTSAKKEV VDWLRQRSRP YLFSNSLAPS IVTASIHVLE MLKSGQALRE
     AVWENSRYFR EKMTEAGFTL GGADHAIIPV MIGDAKLAGD FANRLLEENI YVVGFSFPVV
     PKGQARIRTQ MSAAHTKAQI DRAIEAFTRI AKEMGII
//

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