ID N0B151_9BACI Unreviewed; 408 AA.
AC N0B151;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=UDP-bacillosamine synthetase {ECO:0000313|EMBL:AGK55927.1};
GN ORFNames=B1NLA3E_20945 {ECO:0000313|EMBL:AGK55927.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK55927.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK55927.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK55927.1};
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 -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP005586; AGK55927.1; -; Genomic_DNA.
DR RefSeq; WP_015595968.1; NC_021171.1.
DR AlphaFoldDB; N0B151; -.
DR STRING; 666686.B1NLA3E_20945; -.
DR KEGG; baci:B1NLA3E_20945; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_3_9; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000013300; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000013300}.
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 408 AA; 45810 MW; 708AC4D36120138F CRC64;
MIDTQLRNIP FSPPDITDAE IEEVIKAMKS GWITTGPRTK EFEKRIAEYI GANKAVCLNS
ATAAMELTLR ILGIGPGDEV ITSAYTYTAS ASVIDHVGAK IVLVDTAPNS FEMDYSKLVD
AITEKTKAII PVDIAGKMCD YDTIYKIVNS KKELFKPNNE LQKLFNRVIV MTDAAHAFGA
ERNGLSCGQV GDFTCFSFHA VKNLTTAEGG AVVWCDDLGL DDEWLYKQYM LYSLHGQSKD
ALAKTQKGAW EYDIVYPAYK CNMTDIMAGF GLIQLNRYEG LLKRRQEIIE MYDKAFLPLG
IQSLQHYGED FASSGHLYLV RIPGIGEFER NEIIEKMAEN GIACNVHYKP LPLFTAYKNL
GFHIKDYPNA FDVYKNEITL PLNTLLIDED VEYVIENLMK IMNEVLSD
//
