ID A0A022KTM9_9MICO Unreviewed; 402 AA.
AC A0A022KTM9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Pyridoxal-5'-phosphate-dependent protein {ECO:0000313|EMBL:EYT49316.1};
GN ORFNames=D641_0107730 {ECO:0000313|EMBL:EYT49316.1};
OS Brachybacterium muris UCD-AY4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1249481 {ECO:0000313|EMBL:EYT49316.1, ECO:0000313|Proteomes:UP000019754};
RN [1] {ECO:0000313|EMBL:EYT49316.1, ECO:0000313|Proteomes:UP000019754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-AY4 {ECO:0000313|EMBL:EYT49316.1,
RC ECO:0000313|Proteomes:UP000019754};
RX PubMed=23516213;
RA Lo J.R., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT "Draft genome sequence of an Actinobacterium, Brachybacterium muris strain
RT UCD-AY4.";
RL Genome Announc. 1:E0008613-E0008613(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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:EYT49316.1}.
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DR EMBL; AORC01000009; EYT49316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022KTM9; -.
DR STRING; 1249481.D641_0107730; -.
DR HOGENOM; CLU_033332_2_1_11; -.
DR Proteomes; UP000019754; Unassembled WGS sequence.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000019754}.
FT REGION 382..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 190
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 402 AA; 41901 MW; 939A7123A9AFE32F CRC64;
MMGPRIALSL PVTGQAEQDA VLEALRSGWI TSAGPQLDRF EQELAVHTGR RCAVAVSSGT
AALHLALLAA GAGPGDLVPC STLTFAATAN AICYTGATPV FIDSDATGSM DVSLLDAFLT
DSASAGARVG AVVPVDLFGK IADHAAISRL ADRYGVPVVV DAAESLGSVR EGRPAGSDGR
LAILSFNGNK IITASAGGAV VCDDPALADR VRHLATQARQ PVVHYEHEDI GFNYRLSNLL
AAVGSAQLAR LPEFLAARRA HRDGYRRLAL TLPGVEILGG EDTGDNCWLT AIVIDPAQAG
FDADEAREAL ASHGIESRPV WKPMHLQPVF ADPERYPRLV TGVAEHLFTH GLVLPSGPSM
SHEQRAEVES CLSELSGAAH TVDAQHSAGP AHFGPVGLRS AS
//
