ID A0A0G1FFC6_9BACT Unreviewed; 442 AA.
AC A0A0G1FFC6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=UW04_C0012G0013 {ECO:0000313|EMBL:KKT21060.1};
OS Parcubacteria group bacterium GW2011_GWB1_43_8.
OC Bacteria.
OX NCBI_TaxID=1618874 {ECO:0000313|EMBL:KKT21060.1, ECO:0000313|Proteomes:UP000033953};
RN [1] {ECO:0000313|EMBL:KKT21060.1, ECO:0000313|Proteomes:UP000033953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:KKT21060.1}.
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DR EMBL; LCGU01000012; KKT21060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1FFC6; -.
DR PATRIC; fig|1618874.3.peg.238; -.
DR Proteomes; UP000033953; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KKT21060.1};
KW Transferase {ECO:0000313|EMBL:KKT21060.1}.
FT DOMAIN 48..406
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 442 AA; 49647 MW; 59C60C7E0C99C08A CRC64;
MRNNIVHQGA GELTYEIRGI VDIAEKIKSL GQEIYWENIG DPVANGYQIP EWIKDIVKKA
IDNNKTFAYN PTKGLLSTRE FLAEKRNSKN GAKITADDIC FFNGLGDAIS KIYTYLRKET
RVIGPSPAYS THSSAEAAHA GYPHITYNLL PEKNWLPDLK DLENKIKYNP AISGILIINP
DNPTGMVYPR KVLEQIISLA KKYDLFLISD EVYCNIAHNM KKMTTLAEVI GDVPGIAMKG
ISKEFPWPGS RCGWIEIYNK EKDGIFAKYV KSIMDAKMLE VCSTTLPQSV IPLIMSDPRY
ESHLKERRNF YKKRADKAFK ILKNVPGIIS PKTAGAFYVS VVFKDGVLSL PTGQAGDKQK
LEIKNAKVRK FIEEKTANGI APDKRFVYYL MGATGICVVP LTGFNCNLLG FRATLLEADE
DKFEWIYNTI AQKIKEYLCV GG
//
