ID A0A0C2Y9H7_BACBA Unreviewed; 386 AA.
AC A0A0C2Y9H7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Pleiotropic regulatory protein {ECO:0000313|EMBL:KIL78601.1};
GN ORFNames=SD77_4281 {ECO:0000313|EMBL:KIL78601.1};
OS Bacillus badius.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1455 {ECO:0000313|EMBL:KIL78601.1, ECO:0000313|Proteomes:UP000031982};
RN [1] {ECO:0000313|EMBL:KIL78601.1, ECO:0000313|Proteomes:UP000031982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTCC 1458 {ECO:0000313|EMBL:KIL78601.1,
RC ECO:0000313|Proteomes:UP000031982};
RA Verma A., Khatri I., Mual P., Subramanian S., Krishnamurthi S.;
RT "Genome Assembly of Bacillus badius MTCC 1458.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIL78601.1}.
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DR EMBL; JXLP01000009; KIL78601.1; -; Genomic_DNA.
DR RefSeq; WP_052477316.1; NZ_JXLP01000009.1.
DR AlphaFoldDB; A0A0C2Y9H7; -.
DR STRING; 1455.SD78_0586; -.
DR PATRIC; fig|1455.5.peg.2349; -.
DR Proteomes; UP000031982; Unassembled WGS sequence.
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: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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
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 386 AA; 42989 MW; BFB6AA1BF3E49214 CRC64;
MNIKMLDLSE QYQSMRREVM AKLDEVMSSS QFILGDNVKQ LEADIAKYSG VDHGVGVGNG
SDAIHIALQA AGVEAGDEVI TTAFTFFATG GAIARAGAVP VYVDIDPVTF NISPAKIKAA
ITKKTKAIIP VHLYGQMADM EAIKNIADEH HLAVIEDAAQ AIGAKQNGHS VGELGTAATY
SFFPTKNLGG YGDGGMIVTK DEELAEKARV IRVHGSKPKY YHHVLGYNSR LDEMQAAILN
VKFPYLDKWS HARRERAAYY TDHLQEKLAG VIQTPVQKKG NYHVYHQYTL RVPERDQLQR
YLKEQGVATM VYYPQPLHLQ PVFKQLGYKE GDLPETEKAA KAAISLPMYP ELKQFDQDYV
IEKIVEFYAN KEEEGFNQTK TEEVTQ
//