ID D7BP27_ARCHD Unreviewed; 381 AA.
AC D7BP27;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ADH92676.1};
GN OrderedLocusNames=Arch_0954 {ECO:0000313|EMBL:ADH92676.1};
OS Arcanobacterium haemolyticum (strain ATCC 9345 / DSM 20595 / CCUG 17215 /
OS LMG 16163 / NBRC 15585 / NCTC 8452 / 11018).
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Arcanobacterium.
OX NCBI_TaxID=644284 {ECO:0000313|EMBL:ADH92676.1, ECO:0000313|Proteomes:UP000000376};
RN [1] {ECO:0000313|EMBL:ADH92676.1, ECO:0000313|Proteomes:UP000000376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9345 / DSM 20595 / CCUG 17215 / LMG 16163 / NBRC 15585 /
RC NCTC 8452 / 11018 {ECO:0000313|Proteomes:UP000000376};
RX PubMed=21304742; DOI=10.4056/sigs.1123072;
RA Yasawong M., Teshima H., Lapidus A., Nolan M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J., Bruce D., Detter C., Tapia R.,
RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y., Jeffries C., Rohde M., Sikorski J., Pukall R., Goker M.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Arcanobacterium haemolyticum type strain
RT (11018).";
RL Stand. Genomic Sci. 3:126-135(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP002045; ADH92676.1; -; Genomic_DNA.
DR RefSeq; WP_013170172.1; NC_014218.1.
DR AlphaFoldDB; D7BP27; -.
DR STRING; 644284.Arch_0954; -.
DR KEGG; ahe:Arch_0954; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_11; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000000376; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ADH92676.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000000376};
KW Transferase {ECO:0000313|EMBL:ADH92676.1}.
SQ SEQUENCE 381 AA; 41105 MW; 55BD558DC23A8F2B CRC64;
MSDLIPRYDQ SMMAAYGLPP LVLTRGEGVT VWDSEGRSYL DLDSGGGVTS LGHNHPQLRS
ALLAQAEKIC HVSNSFATEP QVALAERLQQ CLSDEGYLGA TARVFFSNSG SEAMEAALKM
ARLHKPRGRI LTLNRSYHGR TMGALSLADE AYRAPFEPLL SGVQVVQNAA ELESAFDDDV
AACVIDVHHG RSIERLNDHE LGRVRDLCDR FRALLIVDES LSAVGRTGRW FAHTPRVVAD
VITVARGLGG GVPIGVTIGF QTAGRLVQRG LEASSTGGNP LATAAGLCVL NTVEPLLPHV
VRTGAWLKAQ LEALAYEVQG EGLMLAVAVP DAADYERRLR EKGFLVSSTS GEQIRLLPPL
IITRDDLRPF IAAMAELKEY A
//
