ID N0AW47_9BACI Unreviewed; 386 AA.
AC N0AW47;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0000313|EMBL:AGK52656.1};
GN ORFNames=B1NLA3E_04410 {ECO:0000313|EMBL:AGK52656.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK52656.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK52656.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK52656.1};
RX PubMed=23833140;
RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA Brooks S., Kostka J.E., Green S.J.;
RT "Genome sequences for three denitrifying bacterial strains isolated from a
RT uranium- and nitrate-contaminated subsurface environment.";
RL Genome Announc. 1:e00449-13(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP005586; AGK52656.1; -; Genomic_DNA.
DR RefSeq; WP_015592719.1; NC_021171.1.
DR AlphaFoldDB; N0AW47; -.
DR STRING; 666686.B1NLA3E_04410; -.
DR KEGG; baci:B1NLA3E_04410; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_1_9; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000013300; Chromosome.
DR GO; GO:0008483; F:transaminase 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:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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 Aminotransferase {ECO:0000313|EMBL:AGK52656.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000013300};
KW Transferase {ECO:0000313|EMBL:AGK52656.1}.
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 386 AA; 42696 MW; 6A7EF1FE718F3247 CRC64;
MGNLISTKKI YLSSPHMSGN EQKYINEAFE TNWIAPLGPN VDAFENEIAS YIGAKGAVAV
SSGTAAIHLA LSLLDVRKGD TVFCSSLTFI ASANPIVYQG AEPVFIDSEP ETWNMSPNSL
KLALEEANTE GNLPKAVIVV NLYGQSAKMD ELLSICNHYD VPIIEDAAES LGSTYRGIAS
GSFGKYGIYS FNGNKIITTS GGGMLVSNDI EALKKARFLA TQAKDPALHY QHSKTGFNYR
MSNILAGIGR AQLEVLNERV KARRSKFNCY YQELAHLPGF NFMPELKNTY SNRWLTALTI
DENESGISVN SLIKYLAIEN IEARPVWKPL HMQPLFRGAK YYPHRDFQNV SEEIFQSGIC
LPSGSNMSEE EQQRVIHCIR KASNQN
//
