ID A0A0B2K2E6_9FIRM Unreviewed; 388 AA.
AC A0A0B2K2E6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=NZ47_05675 {ECO:0000313|EMBL:KHM52292.1};
OS Anaerovibrio lipolyticus.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Anaerovibrio.
OX NCBI_TaxID=82374 {ECO:0000313|EMBL:KHM52292.1, ECO:0000313|Proteomes:UP000030993};
RN [1] {ECO:0000313|EMBL:KHM52292.1, ECO:0000313|Proteomes:UP000030993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5S {ECO:0000313|EMBL:KHM52292.1,
RC ECO:0000313|Proteomes:UP000030993};
RX PubMed=23950883;
RA Prive F., Kaderbhai N.N., Girdwood S., Worgan H.J., Pinloche E.,
RA Scollan N.D., Huws S.A., Newbold C.J.;
RT "Identification and characterization of three novel lipases belonging to
RT families II and V from Anaerovibrio lipolyticus 5ST.";
RL PLoS ONE 8:E69076-E69076(2013).
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:KHM52292.1}.
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DR EMBL; JSCE01000116; KHM52292.1; -; Genomic_DNA.
DR RefSeq; WP_039207411.1; NZ_JSCE01000116.1.
DR AlphaFoldDB; A0A0B2K2E6; -.
DR STRING; 82374.NZ47_05675; -.
DR eggNOG; COG0436; Bacteria.
DR Proteomes; UP000030993; 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:KHM52292.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030993};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 31..380
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 388 AA; 42873 MW; 59F0EC1AD0BBBBC1 CRC64;
MEFAKRMEQF GEGVFSRLAE MRKERVAAGK NVIDLSIGAP NIPPAKRIME AMAKAVMDPA
NYVYAISDRK AMLDAVARWY QRRYNVTLDP DTEICSLLGS QDGLAHIALS ILDPGDIMMV
PDPCYPIFAD GPRIAGAELY YMPQKKEHDY VIQLGDIPEE VARKAKFMLV SYPNNPTAAM
APIEFYKELV AFAKKYDIIV LHDNAYSELV FDGREWGSFL ELPGAKEVGV EFNSLSKTYG
LAGARIGYCL GNSKVVGMLK TLKSNMDYGM FLPIQAAAIE AISGDQSIVA ETRAAYERRR
DVLCDGLIEA GWQMDKPPGT MFVWAPIPAS YEYSEAFVKD LLDKTGVLVT PGSAFGPSGE
GYVRMALVQS EEDMQRAVDE VKKSGIFA
//
