ID A0A162M888_9FIRM Unreviewed; 399 AA.
AC A0A162M888;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=ATZ99_19420 {ECO:0000313|EMBL:KYO64510.1};
OS Thermovenabulum gondwanense.
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Thermosediminibacteraceae; Thermovenabulum.
OX NCBI_TaxID=520767 {ECO:0000313|EMBL:KYO64510.1, ECO:0000313|Proteomes:UP000075737};
RN [1] {ECO:0000313|EMBL:KYO64510.1, ECO:0000313|Proteomes:UP000075737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R270 {ECO:0000313|EMBL:KYO64510.1,
RC ECO:0000313|Proteomes:UP000075737};
RA Patel B.K.;
RT "Draft genome of Thermovenabulum gondwanense isolated from a red
RT thermophilic microbial mat colonisisng an outflow channel of a bore well.";
RL Submitted (DEC-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|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:KYO64510.1}.
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DR EMBL; LOHZ01000042; KYO64510.1; -; Genomic_DNA.
DR RefSeq; WP_068749043.1; NZ_LOHZ01000042.1.
DR AlphaFoldDB; A0A162M888; -.
DR STRING; 520767.ATZ99_19420; -.
DR PATRIC; fig|520767.4.peg.2067; -.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000075737; 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 PRINTS; PR00753; ACCSYNTHASE.
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:KYO64510.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075737};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KYO64510.1}.
FT DOMAIN 31..391
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 399 AA; 44294 MW; BC7E881FDE2B0F71 CRC64;
MFLSEKAKGI SPSPTLAVDS KAKQMKSEGY DVIGFGAGEP DFDTPSFIKS SAIKAINEGF
TKYTPVGGIP ELKKAIADIF NEELGLTYKP GEIIVSNGAK QCLYNALYCL VNPGDEVLIP
HPYWVSYPEL VKLCGGTPVF VPTYEKDDFK MKKDVIEPLI TSKTRVIVVN SPNNPTGSVY
SKKELEDIAE LAIRYNLFII SDEIYDKLIY DGEKHISIAT LGKEVFNRTL IVNGVSKAYS
MTGWRIGYAA GPEEIVKAMT DFQSHTTSNP NSIAQKAALE ALTNPERKQA ISSMVEEFSK
RRDYMVERIN QIPGLSCIKP KGAFYVMMNI TKTFGKKIKG FEINNSTDFA QKLLENYMVA
VVPGIAFGTE DFVRLSYATS LKNIEKGIDR IENFVRDLV
//
