ID A0A140L6S7_9CLOT Unreviewed; 452 AA.
AC A0A140L6S7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:KXG76252.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:KXG76252.1};
GN ORFNames=AN619_12090 {ECO:0000313|EMBL:KXG76252.1};
OS Thermotalea metallivorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermotalea.
OX NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG76252.1, ECO:0000313|Proteomes:UP000070456};
RN [1] {ECO:0000313|EMBL:KXG76252.1, ECO:0000313|Proteomes:UP000070456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B2-1 {ECO:0000313|EMBL:KXG76252.1,
RC ECO:0000313|Proteomes:UP000070456};
RA Patel B.K.;
RT "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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:KXG76252.1}.
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DR EMBL; LOEE01000028; KXG76252.1; -; Genomic_DNA.
DR RefSeq; WP_068555751.1; NZ_LOEE01000028.1.
DR AlphaFoldDB; A0A140L6S7; -.
DR STRING; 520762.AN619_12090; -.
DR PATRIC; fig|520762.4.peg.1349; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000070456; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KXG76252.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000070456};
KW Transferase {ECO:0000313|EMBL:KXG76252.1}.
SQ SEQUENCE 452 AA; 50726 MW; 7576D48A48003439 CRC64;
MSQNKAPQNH VFYRNQNWHY PKIERGEGVY LYDIHGKRYL DACSGSAVAN IGHGNREIAE
YAAEQMKKIA FTHLSRWTAD PIEECAEKVA RWTPGDLNHV YFVSGGSEAT ETAIKMARQY
FVERDGKDTR KWKVISKWNA FHGNTMGALS MTGIPERRRI YEPMLMDFPK IPQFYHYRNP
WGCKSLEETS RKAAEALEEE ILRQGPENVA AFITEPVVGA ACPGIHPTKT YFEMVREICN
RYDVLLIIDE VMAGFGRTGK KFGIDHYGII PDIMTVAKGM GCGYTPIGAA VASEKIFRRM
MVEGSGQFIH GHTYAGNPLS CGIAAKVIEI LERDCLVENG ARQGEYLMHK LEALYRYPIV
GEIRGKGLMV GIEFVKDQET REPFGVEDNI KGKVTIHCME EGIVPYPGGG SADGIRGDHV
LIAPPLNITE EQIDELVEAL ERGIRKTCRE IG
//
