ID D1W6X8_9BACT Unreviewed; 456 AA.
AC D1W6X8;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase family protein {ECO:0000313|EMBL:EFA91748.1};
GN ORFNames=HMPREF0650_0064 {ECO:0000313|EMBL:EFA91748.1};
OS Hoylesella buccalis ATCC 35310.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=679190 {ECO:0000313|EMBL:EFA91748.1, ECO:0000313|Proteomes:UP000005283};
RN [1] {ECO:0000313|EMBL:EFA91748.1, ECO:0000313|Proteomes:UP000005283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35310 {ECO:0000313|EMBL:EFA91748.1,
RC ECO:0000313|Proteomes:UP000005283};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA Nelson K.E.;
RT "Genome Sequence of Prevotella buccalis ATCC 35310.";
RL Submitted (DEC-2009) 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 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:EFA91748.1}.
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DR EMBL; ADEG01000073; EFA91748.1; -; Genomic_DNA.
DR RefSeq; WP_004349880.1; NZ_ADEG01000073.1.
DR AlphaFoldDB; D1W6X8; -.
DR STRING; 679190.HMPREF0650_0064; -.
DR eggNOG; COG0399; Bacteria.
DR Proteomes; UP000005283; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 2.
DR PIRSF; PIRSF000390; PLP_StrS; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EFA91748.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Transferase {ECO:0000313|EMBL:EFA91748.1}.
FT REGION 56..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 235
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 456 AA; 50740 MW; F7D9F50030E39A96 CRC64;
MNKRIYLCLA HMSGNEMKYI QEAFDTNWVV PLGPNVNAFE EELKRFIAST DCSSGRGECD
RDKQRREDYP QSIAPHENDP EKLWLKGDER LKDKQVVALA SGTSAIHLAL VVLGVKAGDE
VICQSFTFCA SSHPVTYQGA TPVFVDSEND SWNMDPELLE EAIKDRIEKT GRKPKAIIVV
YLYGMPAKIQ EIQAVAQKYD IPLIEDAAEG LGSRYKGQVV GTFGRFGVLS FNGNKMITTS
GGGALICPDE ETKNRVMFFA TQAREAFPYY EHEEIGYNYR LSNVCAGIGR GQLTVLDEHI
AHHRHLADLY EEAFKDVEGI TFHTNPSTDF DSNYWLNTIT LDSELQVKGQ EHAYEQAVKG
AVGGAAGVVH ATGKVHTSCE PNANVEAMRV ALDKMGIESR PLWKPMHLQP VYKNCPAYTN
GVSEQLFKIG MCLPSGPYVS ENDARYIVQS IIDQIK
//
