ID   A0A0T5ZLP2_9BACT        Unreviewed;       389 AA.
AC   A0A0T5ZLP2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=XU11_C0061G0011 {ECO:0000313|EMBL:KRT63740.1};
OS   Candidatus Dadabacteria bacterium CSP1-2.
OC   Bacteria; Thermodesulfobacteriota; Candidatus Dadabacteria.
OX   NCBI_TaxID=1640508 {ECO:0000313|EMBL:KRT63740.1, ECO:0000313|Proteomes:UP000051780};
RN   [1] {ECO:0000313|EMBL:KRT63740.1, ECO:0000313|Proteomes:UP000051780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-2 {ECO:0000313|EMBL:KRT63740.1};
RA   Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA   Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT   "Critical biogeochemical functions in the subsurface are associated with
RT   bacteria from new phyla and little studied lineages.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         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:KRT63740.1}.
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DR   EMBL; LDXN01000061; KRT63740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T5ZLP2; -.
DR   STRING; 1640508.XU11_C0061G0011; -.
DR   PATRIC; fig|1640508.3.peg.2351; -.
DR   Proteomes; UP000051780; 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   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR46383:SF2; (5-FORMYLFURAN-3-YL)METHYL PHOSPHATE TRANSAMINASE; 1.
DR   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 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:KRT63740.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KRT63740.1}.
FT   DOMAIN          30..372
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   389 AA;  43544 MW;  57049E6442D31C49 CRC64;
     MPSKLSEEIA PFFVMDVLER AKEIEAQGKR VIHFEIGEPD LPTPNIICDE AIEAIRIGDT
     KYTPSLGIPE LREAIAEDYK EKYGVNITPG RVVITSGSSP ALFLSMLSLL EHGDEVIITD
     PHYSCYPQII KVAGGLPKRV RIYEEDGFQI DIDSLKKTIS SKTKAIVINS PSNPTGVVLE
     PNVIKEISEL GLYIISDEIY HGLVYEGKAH TILEFTDKAF SVNGFSKLYS MTGWRLGYFI
     APDDFIRPIQ KLQQNLFISP NPFVQRAGVA AIRKAKREAK EMVQIFSERR KKMIEGLRGL
     GFVIRSEPKG AFYVFVNAKS LNDRSQELAF DILEKSHVAV TPGIDFGYGG EGYLRFSYTT
     SLDDIEEGIK RLGEYIKGKI NAHKELIES
//