ID C5TBE5_ACIDE Unreviewed; 394 AA.
AC C5TBE5;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=AcdelDRAFT_4225 {ECO:0000313|EMBL:EER58207.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER58207.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER58207.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER58207.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) 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 -!- 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:EER58207.1}.
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DR EMBL; ACQT01000325; EER58207.1; -; Genomic_DNA.
DR RefSeq; WP_005799981.1; NZ_ACQT01000325.1.
DR AlphaFoldDB; C5TBE5; -.
DR PATRIC; fig|573060.9.peg.710; -.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000003856; 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; 3.40.640.10; 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 PANTHER; PTHR46383:SF2; (5-FORMYLFURAN-3-YL)METHYL PHOSPHATE TRANSAMINASE; 1.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 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:EER58207.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003856};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EER58207.1}.
FT DOMAIN 36..389
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 394 AA; 43192 MW; 0F04A23A5ECDD98F CRC64;
MKFSTRAERI EPFYVMEVAK AAQALAREVA GSSDPMIFLN IGEPDFTAPP LVQEAAARAV
RDGATQYTQS LGHEPLRERI SDWYQQRFGV NVPARRIVVT AGASAALHLA CLALIEAGDE
VLMPDPSYPC NRHFVSAAEG NAVLIPTTAA ERYQLSADKV RAAWNPRTRG VLLASPSNPT
GTSIAPDELR RIHGVVQEHG GITLIDEIYL GLSYDDAFGQ TALAIDDNVI SINSFSKYFN
MTGWRLGWMV VPDAMVPVVE RLAQNLFICA STVSQLAAMA CFEAESIAEY ERRRAEFKAR
RDYFIPELQA LGLAVPVMPD GAFYAWADCA SACKQLGVQG SWDFAYEVMR RAHVAVTPGR
DFGTAETHHF VRFSTANSMA QLQESVARLR GLLG
//
