ID A0A160F662_9BACI Unreviewed; 370 AA.
AC A0A160F662;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Beta-eliminating lyase family protein {ECO:0000313|EMBL:ANB61661.1};
GN ORFNames=GFC30_479 {ECO:0000313|EMBL:ANB61661.1};
OS Anoxybacillus amylolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB61661.1, ECO:0000313|Proteomes:UP000076865};
RN [1] {ECO:0000313|EMBL:ANB61661.1, ECO:0000313|Proteomes:UP000076865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB61661.1,
RC ECO:0000313|Proteomes:UP000076865};
RX PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA Gambacorta A., Nicolaus B.;
RT "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT bacterium isolated from Mount Rittmann (Antarctica).";
RL Syst. Appl. Microbiol. 29:300-307(2006).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP015438; ANB61661.1; -; Genomic_DNA.
DR RefSeq; WP_066322729.1; NZ_CP015438.1.
DR AlphaFoldDB; A0A160F662; -.
DR KEGG; aamy:GFC30_479; -.
DR PATRIC; fig|294699.3.peg.473; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000076865; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ANB61661.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000076865}.
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 186
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 370 AA; 41311 MW; 35988992135D2DF5 CRC64;
MKVPMLDLSE QYQRLRTEML TVLDEVMSSS RFILGDHVKK LENDVAAYSN VKHGIGCGNG
SDAIHIALQA IGVGPGDEVI TTPFTFFATG GAIVRAGAKP VFVDIDPVTF NIDPAKIEEA
ITEKTKAILP VHLYGQMADM DPIVEIANKR GLFIIEDAAQ AIGAKYKGKN VGELGTAATY
SFFPTKNLGA YGDGGMIVTN DEEIAEKCRV IRVHGSKPKY YHHVLGYNSR LDEMQAAILN
VKFPHLNEWS ELRRERAATY THLLKEMLGD VVVTPVEVDG HYHVFHQYTI RVPKRDELQA
FLKENGVSTM VYYPLPLHLQ PVFQELGYKE GDLPEAEKAA KEAVSLPMFP ELKVEQQQYV
VEKIVEFYKK
//
