ID A0A098QYW0_9SPIO Unreviewed; 474 AA.
AC A0A098QYW0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Aminotransferase class III {ECO:0008006|Google:ProtNLM};
GN ORFNames=DC28_05400 {ECO:0000313|EMBL:KGE72814.1};
OS Spirochaeta lutea.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=1480694 {ECO:0000313|EMBL:KGE72814.1, ECO:0000313|Proteomes:UP000029692};
RN [1] {ECO:0000313|EMBL:KGE72814.1, ECO:0000313|Proteomes:UP000029692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC230 {ECO:0000313|EMBL:KGE72814.1,
RC ECO:0000313|Proteomes:UP000029692};
RA Shivani Y., Subhash Y., Tushar L., Sasikala C., Ramana C.V.;
RT "De novo Genome Sequence of Spirocheata sp.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KGE72814.1}.
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DR EMBL; JNUP01000047; KGE72814.1; -; Genomic_DNA.
DR RefSeq; WP_037546635.1; NZ_JNUP01000047.1.
DR AlphaFoldDB; A0A098QYW0; -.
DR STRING; 1480694.DC28_05400; -.
DR eggNOG; COG0001; Bacteria.
DR OrthoDB; 366836at2; -.
DR Proteomes; UP000029692; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
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; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000029692}.
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 50471 MW; A0225355EC068366 CRC64;
MQNSRRPQVP PHHTVQPNPV SGANPTKRGD DALGTPGISQ QSRAQENGNP LPNGLSAANF
SGLSIHPLII TSASGCRFKD TTGKDYIDFT SGEGSAILGF GGTRFYQPCT GLQNPDGALR
GEVKSDTPKA ASRAGGSPSD AFEAGCLDRL PEPSSLTITL AQKLTETIQG TTWTAITHDG
TSAVEAAVAL ARQETGKRLI LLPRDSRQTA YPFCLSGQRT FPLNLLGPDQ IQTLVYGDEP
ALEELFRRHR GKIAAVLLPP YLEPASDHAV MPHGTWYTRV ESLCRQEGAL FILDDLDTTL
RLSLHGSHAY FGAHPDLICL GSTLANGLPM GVLLGTKALE SAGSRIPREF FHPVNTASIS
AALGTLETLG SQNHMEILQL RGQSLRRGLH EIAGEAGLSL SITGPPAVPS IRIAGDPQGL
LNPSLSRHCI SQGVYLAPHR GTFLSLAHNE ADLELAMERL GPAFANFARE NSLS
//
