ID Q1DC11_MYXXD Unreviewed; 429 AA.
AC Q1DC11;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Aminotransferase, class I {ECO:0000313|EMBL:ABF92615.1};
GN OrderedLocusNames=MXAN_1560 {ECO:0000313|EMBL:ABF92615.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF92615.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF92615.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; CP000113; ABF92615.1; -; Genomic_DNA.
DR RefSeq; WP_011551671.1; NC_008095.1.
DR AlphaFoldDB; Q1DC11; -.
DR STRING; 246197.MXAN_1560; -.
DR EnsemblBacteria; ABF92615; ABF92615; MXAN_1560.
DR GeneID; 41359005; -.
DR KEGG; mxa:MXAN_1560; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_034385_1_0_7; -.
DR OrthoDB; 9770700at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABF92615.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Transferase {ECO:0000313|EMBL:ABF92615.1}.
FT DOMAIN 36..411
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 429 AA; 47653 MW; 75A5C1E8F2598E80 CRC64;
MSDDVPLPAF RAVPRTGVIF VTAEATRRGY RSSNPEWCNL GQGQPETGDL PGAPPRLNQV
TIDVADMEYA PVAGLWEVRE SIASLYNRLY RRGMPSQYSA ENVCLSGGGR AALTRAAASL
GAINLGHFLP DYTAYEELLD VFKAFTAIPI LLEGERGYAF TAEDLRREVQ GRGLSALLFS
NPCNPTGKLV HGEEMARWVS VAREHECALL VDEFYSHYIW TGRPGHLPVE SAARYVEDVN
KDPVVLFDGF TKNWRYPGWR MTWTVGPRQV IDAVASAGSF LDGGGSRPLQ RAAIQLLQEE
PVVAETMAIH NTFREKRDRF HSRLERIGIR TDRAPDGTFY VWGNVSGLPP PLNDGMGFFR
AALDQKIIAV PGEFFDVNPG KRRARPSRFR GYVRLSFGPS METLEKALSR LEAMVLHYSR
TPGQPPPAP
//