ID E3I1Q0_RHOVT Unreviewed; 408 AA.
AC E3I1Q0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=Rvan_3230 {ECO:0000313|EMBL:ADP72425.1};
OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS 4299).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Rhodomicrobium.
OX NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP72425.1, ECO:0000313|Proteomes:UP000001399};
RN [1] {ECO:0000313|Proteomes:UP000001399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC {ECO:0000313|Proteomes:UP000001399};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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}.
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DR EMBL; CP002292; ADP72425.1; -; Genomic_DNA.
DR RefSeq; WP_013420784.1; NC_014664.1.
DR AlphaFoldDB; E3I1Q0; -.
DR STRING; 648757.Rvan_3230; -.
DR KEGG; rva:Rvan_3230; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_5; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000001399; 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:ADP72425.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001399};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ADP72425.1}.
FT DOMAIN 32..384
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 408 AA; 44740 MW; B4A59E2911DD5AA7 CRC64;
MTEEFHRIKR LPPYVFEQVN KLKAAARARG EDIIDLGMGN PDLPTPDHIT EKLIETVGKP
RTNRYSASRG IPGLRRAQAG YYDRRFGVKL NPDTQVVATL GSKEGFANMA QAITAPGDLV
LVPSPTYPIH EFGFIISGGT IRHVPASVDD TFLSAVDKAV KHSVPKPLAL IISYPSNPTA
LMASLDFYKE VIDYAKKHDL IVLSDVAYAE IYFDDNPPPS ILQVPGAFDV AVEFTSLSKT
YSMPGWRMGF CVGNERLCAA LARVKSYLDY GAFTPIQVAA TAALNGPQDC VEEMRQIYKR
RRDCLVETFE RAGWPIPAPG GTMFAWAPLP PGWEKVGSLE FSKLLLEKAG VAVSPGLGFG
EYGEGFVRIA LVENEHRIRQ AARAVKKFLS SGEQTLHNVI PFAEAGAR
//
