ID A0A017RTW4_9CLOT Unreviewed; 394 AA.
AC A0A017RTW4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=Q428_09230 {ECO:0000313|EMBL:EYE88203.1};
OS Fervidicella metallireducens AeB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Fervidicella.
OX NCBI_TaxID=1403537 {ECO:0000313|EMBL:EYE88203.1, ECO:0000313|Proteomes:UP000019681};
RN [1] {ECO:0000313|EMBL:EYE88203.1, ECO:0000313|Proteomes:UP000019681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AeB {ECO:0000313|EMBL:EYE88203.1,
RC ECO:0000313|Proteomes:UP000019681};
RX PubMed=24786951;
RA Patel B.K.;
RT "Draft Genome Sequence of Fervidicella metallireducens Strain AeBT, an
RT Iron-Reducing Thermoanaerobe from the Great Artesian Basin.";
RL Genome Announc. 2:e00345-14(2014).
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:EYE88203.1}.
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DR EMBL; AZQP01000026; EYE88203.1; -; Genomic_DNA.
DR RefSeq; WP_035380127.1; NZ_AZQP01000026.1.
DR AlphaFoldDB; A0A017RTW4; -.
DR STRING; 1403537.Q428_09230; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000019681; 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:EYE88203.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019681};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EYE88203.1}.
FT DOMAIN 31..389
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 394 AA; 43471 MW; F009F1B9F47970E6 CRC64;
MELSRKGQQI SSSITLAITA KAKKLKEEGV DVISFGAGEP DFNTPKNIQD VAVDAIRNGL
TRYTPASGIL ELKNAICTKL REENSIDYIP SQIVVSNGAK QSIANALMAI CNPGDEVIVP
VPYWVSYPEL VKLADATPVY VETSEKNNFK YTKDDILKAL TNKTKAIILN SPNNPTGTVY
SKEDLEMIAD IAIKNDIIVI SDEIYEKLVY GSVKHISIAS LNEEIKKRTI VINGVSKAYA
MTGWRIGYTA SNEEIAKIMS NIQSHVTSNP NTIAQYASVE AINGPQEDVE KMRIEFEKRR
DYMVERINSI PGISCNMPDG AFYVMINITN IKGKVVKGYQ INSSFDFCNA LLEIEKVAAI
PGAAFGADDF VRLSYATSME IIQKGLDRIE NFLK
//
