ID A3XI48_LEEBM Unreviewed; 382 AA.
AC A3XI48;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=MED217_15930 {ECO:0000313|EMBL:EAQ51047.1};
OS Leeuwenhoekiella blandensis (strain CECT 7118 / CCUG 51940 / KCTC 22103 /
OS MED217) (Flavobacterium sp. (strain MED217)).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Leeuwenhoekiella.
OX NCBI_TaxID=398720 {ECO:0000313|EMBL:EAQ51047.1, ECO:0000313|Proteomes:UP000001601};
RN [1] {ECO:0000313|EMBL:EAQ51047.1, ECO:0000313|Proteomes:UP000001601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED217 {ECO:0000313|EMBL:EAQ51047.1,
RC ECO:0000313|Proteomes:UP000001601};
RX PubMed=17215843; DOI=10.1038/nature05381;
RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA Neutze R., Pedros-Alio C., Pinhassi J.;
RT "Light stimulates growth of proteorhodopsin-containing marine
RT Flavobacteria.";
RL Nature 445:210-213(2007).
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:EAQ51047.1}.
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DR EMBL; AANC01000001; EAQ51047.1; -; Genomic_DNA.
DR RefSeq; WP_009781526.1; NZ_CH672395.1.
DR AlphaFoldDB; A3XI48; -.
DR STRING; 398720.MED217_15930; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_10; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000001601; 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:SF3; LL-DIAMINOPIMELATE 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:EAQ51047.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001601};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 33..381
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 382 AA; 41919 MW; E8F387B0556A5A17 CRC64;
MIIASANRLN QTSEYYFSRK LKEVRALAAA GKPIINMGIG SPDLAPPPHV IKALTSSLVD
GPAHQYQSYK GLPQLTEAMA DFYQKRYAVT LNPEDEILPL MGSKEGIMHI SMAFLNPGDE
VLIPNPGYPT YTSVTRLVEA EPVYYNLDAS NNWMPDYSAL EKRDLSKVKL MWVNYPHMPT
GAKATTADFE KLVAFAKANE ILLVNDNPYS FILNENPQSI LSVSGAKEVA IELNSLSKSF
NMSGWRVGML LGAADYVSTV LTVKSNMDSG MFYGIQKGAA AVLTEGEAWF DGLNAIYEKR
REQVWKLADV LGCTYDKNAA GMFVWAKLPE GAGAAEAFID DILINKSVFI TPGSIFGSQG
AGYIRFSLCV TEDKIKEAIG RF
//
