ID A0A258TLA4_9PROT Unreviewed; 396 AA.
AC A0A258TLA4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=B7Y41_16635 {ECO:0000313|EMBL:OYY92238.1};
OS Hydrogenophilales bacterium 28-61-23.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970530 {ECO:0000313|EMBL:OYY92238.1, ECO:0000313|Proteomes:UP000215898};
RN [1] {ECO:0000313|EMBL:OYY92238.1, ECO:0000313|Proteomes:UP000215898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-61-23 {ECO:0000313|EMBL:OYY92238.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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|ARBA:ARBA00007441,
CC 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:OYY92238.1}.
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DR EMBL; NCGJ01000029; OYY92238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258TLA4; -.
DR Proteomes; UP000215898; 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; 3.90.1150.10; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:OYY92238.1};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:OYY92238.1}.
FT DOMAIN 30..391
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 396 AA; 42122 MW; 25D3FABBFC094DC6 CRC64;
MELSRRVQNI KPSPTLAVSA RAAKMKAEGK DIIGLGVGEP DFDTPQHIKD AAIAAIHAGF
TKYTAVGGTP SLKKAVIDKF KRENGLEYQA NQVLVSCGGK QSFYNLAQAF INPGDEVIIP
APYWVSYPDM VILADGVPVI VDAGIEQGFK ITPAQLEASI TPKTKMLVIN SPSNPSGAVY
SKAELAALGE VLRRHPQVLI VSDDMYEHIL MGEGEYSNIL NACPDLYGQT MVLNGVSKAY
AMTGWRIGYA AGPREIIAAM DNIQSQSTSN PTSISQVAAE MALNGDQSCI TPMLSAFRER
HRFVVDALNA IPGVNCVDSG GAFYAFPDVS AAIAKLHADG KLAAANDMAL TERLLEFGVA
LVPGSAFGSE GCIRISFATS MDNLKKAIER IAQALA
//
