ID U4KSK5_9MOLU Unreviewed; 372 AA.
AC U4KSK5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Aminotransferase family protein, pyridoxal phosphate-dependent {ECO:0000313|EMBL:CCV65099.1};
GN ORFNames=BN85300780 {ECO:0000313|EMBL:CCV65099.1};
OS Paracholeplasma brassicae.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Paracholeplasma.
OX NCBI_TaxID=61635 {ECO:0000313|EMBL:CCV65099.1, ECO:0000313|Proteomes:UP000032737};
RN [1] {ECO:0000313|EMBL:CCV65099.1, ECO:0000313|Proteomes:UP000032737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0502 {ECO:0000313|Proteomes:UP000032737};
RX PubMed=24158107; DOI=10.1159/000354322;
RA Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
RA Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
RT "Analysis of the Complete Genomes of Acholeplasma brassicae , A. palmae and
RT A. laidlawii and Their Comparison to the Obligate Parasites from '
RT Candidatus Phytoplasma'.";
RL J. Mol. Microbiol. Biotechnol. 24:19-36(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; FO681348; CCV65099.1; -; Genomic_DNA.
DR RefSeq; WP_030003969.1; NC_022549.1.
DR AlphaFoldDB; U4KSK5; -.
DR STRING; 61635.BN85300780; -.
DR KEGG; abra:BN85300780; -.
DR HOGENOM; CLU_033332_2_1_14; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000032737; Chromosome Acholeplasma brassicae.
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:CCV65099.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000032737};
KW Transferase {ECO:0000313|EMBL:CCV65099.1}.
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 372 AA; 41960 MW; CD1940423C1B70E5 CRC64;
MEKKILLSSP HMSAEGYEQE YVKEAFDTNW VAPLGPNVNG FENEIAVKVG IGHAAALVSG
TAAIHMALKA AGVKEGDIVL CQSLTFSATA NPIIYEKAIP VFVDSDYETW NMSPKFLEEA
LIKYPNTKVV LVVHLYGLSA DMDKIVALCK KHNVTLIEDA AESLGTTFKG RYTGTLGDYG
IFSFNGNKII TTSGGGMLVS NNAERIQKVR FWSTQARNQA RHYQHSELGY NYRMSNVVAG
IGRGQLKVLD QRVEKKRQIY QYYKESLKDI KEIEFMPMND WNYSNCWLTS ITLKGKVTPV
DLIIALEKEN IESRPLWKPM HLQPFFEKYD FIGDRTSDDL FNRGLCLPSD SKMTIEEQNR
VIKAIKEVFK NA
//
