ID   D1W053_9BACT            Unreviewed;       608 AA.
AC   D1W053;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=HMPREF9019_0042 {ECO:0000313|EMBL:EFA97234.1};
OS   Hoylesella timonensis CRIS 5C-B1.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hoylesella.
OX   NCBI_TaxID=679189 {ECO:0000313|EMBL:EFA97234.1, ECO:0000313|Proteomes:UP000004001};
RN   [1] {ECO:0000313|EMBL:EFA97234.1, ECO:0000313|Proteomes:UP000004001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRIS 5C-B1 {ECO:0000313|EMBL:EFA97234.1,
RC   ECO:0000313|Proteomes:UP000004001};
RA   Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA   Nelson K.E.;
RT   "Genome Sequence of Prevotella timonensis CRIS 5C-B1.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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:EFA97234.1}.
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DR   EMBL; ADEF01000044; EFA97234.1; -; Genomic_DNA.
DR   RefSeq; WP_008124556.1; NZ_ADEF01000044.1.
DR   AlphaFoldDB; D1W053; -.
DR   GeneID; 78330435; -.
DR   eggNOG; COG0079; Bacteria.
DR   eggNOG; COG1213; Bacteria.
DR   Proteomes; UP000004001; Unassembled WGS sequence.
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   ECO:0000313|EMBL:EFA97234.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004001};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EFA97234.1}.
FT   DOMAIN          3..122
FT                   /note="MobA-like NTP transferase"
FT                   /evidence="ECO:0000259|Pfam:PF12804"
FT   DOMAIN          315..600
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   608 AA;  70517 MW;  F128F23953C8E575 CRC64;
     MQAIILAAGM GRRLGSYTKE NTKCMVPVNG VKLIDRVLTQ LSQLNLQRVI IVVGYKGQEL
     IKYLDHRYDD KLKIEFVNNP IYDRTNNIYS LSLVKDQMQE DDTILIESDL IFSDRLFSMI
     LADERPNIAL VAKYETWMDG TMVRIDGDGN IVNFVPKKAF NYQEVDSYYK TVNIYKFSKT
     FSQTQYVPFL DAYCKALGNN EYYEQVLRVI TLLDKTNLKA LDIGNEKWYE IDDVQDLDIA
     ETIFAKDDEM LKRYNYRYGG HWRFPKMLDY CYLVNPYFPC EQMKAEMKAN FDTLLTEYPS
     GMYVNSLLAG KCFGIKQEYM VVGNGAAELI KSLMENVKGN VGMVFPTFEE YPHRLRKEQI
     VAFVPPLDTL RYTANDLMNF YKDKSIDMLL LINPDNPSGN FIPKADVVRL AAWCKERNIQ
     LVVDESFVDF SDDFLHNSLL CDETLEAYPN LLVMKSISKS YGVPGLRLGI LATSQRETIA
     RIKKDVSIWN INSFAEFFMQ IYNKYQAQYE KACQQFIDER NRFALRLKEI HFLRVLPTQA
     NYFCCEVKPP YTAAELTKQL LARFDIMIKD CNSKTSLKGL NYIRISIRNQ ADNDQLITAL
     LNLQNETI
//