ID   A6LC08_PARD8            Unreviewed;       605 AA.
AC   A6LC08;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=BDI_1465 {ECO:0000313|EMBL:ABR43222.1};
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR43222.1, ECO:0000313|Proteomes:UP000000566};
RN   [1] {ECO:0000313|EMBL:ABR43222.1, ECO:0000313|Proteomes:UP000000566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC   {ECO:0000313|Proteomes:UP000000566};
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; CP000140; ABR43222.1; -; Genomic_DNA.
DR   RefSeq; WP_008780419.1; NC_009615.1.
DR   AlphaFoldDB; A6LC08; -.
DR   STRING; 435591.BDI_1465; -.
DR   PaxDb; 435591-BDI_1465; -.
DR   KEGG; pdi:BDI_1465; -.
DR   PATRIC; fig|435591.13.peg.1452; -.
DR   eggNOG; COG0079; Bacteria.
DR   eggNOG; COG1213; Bacteria.
DR   HOGENOM; CLU_451177_0_0_10; -.
DR   BioCyc; PDIS435591:G1G5A-1506-MONOMER; -.
DR   Proteomes; UP000000566; 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   CDD; cd02523; PC_cytidylyltransferase; 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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR025877; MobA-like_NTP_Trfase.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR42885:SF1; THREONINE-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF12804; NTP_transf_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000566};
KW   Transferase {ECO:0000256|RuleBase:RU000481}.
FT   DOMAIN          3..135
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
FT   DOMAIN          295..600
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   605 AA;  69701 MW;  431A8E9E74965F18 CRC64;
     MQAIILAAGM GKRLKELTKN NTKCMIKVHN QTLIERMLKQ LEALSLKRII IVIGYKGEKV
     RELIGDKINN TPVLYVENNV YDKTNNIYSL YLAKNYLVED ETILLESDLI FENSILSKLI
     NHPYPNLAVV AKYQSWMDGT VVRLDEDNNI LNFISKKAFQ FCQKESYYKT VNIYKFSKEF
     STNKYIPFLE AYCKALGNNE YYEQVLKVIS LLDRPDLKAL TITTEKWYEI DDQQDLNNAE
     ALFSEGKQAL SLYGKRYGGY WRFPMLLDFC YLVNPYFPNT RLKEEMKANF DTLLTEYPSG
     MQENAQLAAR YAGISSEQII VGNGAAELIS GYMRMTSKYT TGVILPTFEE YPNRLAPKQL
     VYYTPSNRDF SYTALDIISF FDNKAIEQLL IINPDNPSGN LLSKNEIFAL VEWSERKGIR
     LIIDESFLDF ANPENKLSLL DKELLNKYPH LIVIKSISKS YGVPGLRLGF LASGNKDLIR
     TLKKDISIWN INSFAEFYMQ IFVKYSDDYD KACHKFLNER ERFFQNLQAV SYLRVIPSAA
     NYFLCEVTDT YTSEELCSSL LSGNNILIKN CGTKAGFEGK QYIRIAIRNK EDNDKLIEAL
     TSLNK
//