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Database: UniProt
Entry: Q1DC11_MYXXD
LinkDB: Q1DC11_MYXXD
Original site: Q1DC11_MYXXD 
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
//
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