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Database: UniProt
Entry: A0A0N1ALV0_9SPHN
LinkDB: A0A0N1ALV0_9SPHN
Original site: A0A0N1ALV0_9SPHN 
ID   A0A0N1ALV0_9SPHN        Unreviewed;       399 AA.
AC   A0A0N1ALV0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=IP65_11665 {ECO:0000313|EMBL:KPF54470.1};
OS   Novosphingobium sp. AAP1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1523413 {ECO:0000313|EMBL:KPF54470.1, ECO:0000313|Proteomes:UP000037880};
RN   [1] {ECO:0000313|EMBL:KPF54470.1, ECO:0000313|Proteomes:UP000037880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP1 {ECO:0000313|EMBL:KPF54470.1,
RC   ECO:0000313|Proteomes:UP000037880};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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:KPF54470.1}.
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DR   EMBL; LJHO01000004; KPF54470.1; -; Genomic_DNA.
DR   RefSeq; WP_054131884.1; NZ_LJHO01000004.1.
DR   AlphaFoldDB; A0A0N1ALV0; -.
DR   STRING; 1523413.IP65_11665; -.
DR   PATRIC; fig|1523413.3.peg.3385; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000037880; 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; 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:KPF54470.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037880};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KPF54470.1}.
FT   DOMAIN          32..384
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   399 AA;  43683 MW;  55ACF02CC9008C91 CRC64;
     MEEEFYRIKR LPPYVIAEVN AMRAAARASG RDIIDLGMGN PDLPPPAHVI EKLCEVAQKP
     SAHGYSASKG IPGIRKAQAN YYATRFNVEL DPETEVVMTM GSKEGLASLA TAITAPGDVV
     LAPNPSYPIH TFGFIIAGAT IRSVPTTPDE RYWESLDRAM AFTVPRPSIL IVNYPSNPTA
     ETVDLAFYER LVAWAKENKV WILSDLAYSE LYFDGQPTRS ILEVPGAKDV AVEFTSMSKT
     FSMAGWRVGF AVGNKRLIAA LTRVKSYLDY GAFTPIQAAA CAALNGPQDI VEQNRKLYQK
     RRDVMVEAFG RAGWEIPSPK ASMFAWAPLP PALKHMGSLE FSKQLLTQAE VAVAPGVGYG
     EDGEGFVRIA MVENEQRLRQ AARNIKRYLT SMGVNASAA
//
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