ID A5FY28_ACICJ Unreviewed; 403 AA.
AC A5FY28;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=Acry_1299 {ECO:0000313|EMBL:ABQ30510.1};
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ30510.1, ECO:0000313|Proteomes:UP000000245};
RN [1] {ECO:0000313|EMBL:ABQ30510.1, ECO:0000313|Proteomes:UP000000245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ30510.1,
RC ECO:0000313|Proteomes:UP000000245};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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|RuleBase:RU000481}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000697; ABQ30510.1; -; Genomic_DNA.
DR RefSeq; WP_007423251.1; NC_009484.1.
DR AlphaFoldDB; A5FY28; -.
DR STRING; 349163.Acry_1299; -.
DR KEGG; acr:Acry_1299; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_5; -.
DR Proteomes; UP000000245; Chromosome.
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; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF1; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAC; 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:ABQ30510.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000245};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ABQ30510.1}.
FT DOMAIN 32..383
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 403 AA; 44139 MW; 33EB06ED6B6A11F8 CRC64;
MTEEFHRIRR LPPYVFAEVN QAKAAARNRR EDIIDLGMGN PDSATPPHIV AKLVETVADP
RSHRYSTSKG IPGLRRALAA YYDRRFGVKL NPETEVIATL GSKEGLANLA NAITSPGDTI
LVPNPSYPIH QFGFIIAGAS VRSVPATPDD EMLRALDRAV RHSVPKPTAL IVNFPSNPTA
YLATLDFYKE IVAFARKHEI FILSDLAYAE IYFEGEPPPS VLQVEGAKDI TVEFTSMSKT
YSMPGWRMGF AAGNPRLVAA LARMKSYLDY GAFTPIQVAA TAALNGPQDC VEQMRTLYRE
RRDVLIKGLA QAGWDVPSPA GSMFAWAPIP ERFAHLGSVD FAKLLLERAK VAVAPGIGFG
EYGDGHVRIA LVENTHRLRQ AVRNIRAFMA PGNAPNQQES VSA
//
