ID A0A0B4S3P0_9FIRM Unreviewed; 396 AA.
AC A0A0B4S3P0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Capsular biosynthesis protein {ECO:0000313|EMBL:AIZ37189.1};
DE SubName: Full=DegT/DnrJ/EryC1/StrS family aminotransferase {ECO:0000313|EMBL:MBF1307188.1};
GN ORFNames=HXM94_05380 {ECO:0000313|EMBL:MBF1307188.1}, NW74_07565
GN {ECO:0000313|EMBL:AIZ37189.1};
OS Parvimonas micra.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Parvimonas.
OX NCBI_TaxID=33033 {ECO:0000313|EMBL:AIZ37189.1, ECO:0000313|Proteomes:UP000031386};
RN [1] {ECO:0000313|EMBL:AIZ37189.1, ECO:0000313|Proteomes:UP000031386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCOM 1535 {ECO:0000313|EMBL:AIZ37189.1}, and KCOM 1535 / ChDC
RC B708 {ECO:0000313|Proteomes:UP000031386};
RA Kook J.-K., Park S.-N., Lim Y.K., Roh H.;
RT "Complete genome sequence of Parvimonas micra KCOM 1535 (= ChDC B708).";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBF1307188.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCVI_23_bin.11 {ECO:0000313|EMBL:MBF1307188.1};
RA Baker J.L., Morton J.T., Dinis M., Alvarez R., Tran N.C., Knight R.,
RA Edlund A.;
RT "Deep metagenomics examines the oral microbiome during advanced dental
RT caries in children, revealing novel taxa and co-occurrences with host
RT molecules.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP009761; AIZ37189.1; -; Genomic_DNA.
DR EMBL; JABZRE010000018; MBF1307188.1; -; Genomic_DNA.
DR RefSeq; WP_004832560.1; NZ_RKIS01000001.1.
DR AlphaFoldDB; A0A0B4S3P0; -.
DR STRING; 33033.NW74_07565; -.
DR KEGG; pmic:NW74_07565; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000031386; Chromosome.
DR Proteomes; UP000758611; 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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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 Aminotransferase {ECO:0000313|EMBL:MBF1307188.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000031386};
KW Transferase {ECO:0000313|EMBL:MBF1307188.1}.
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 396 AA; 44472 MW; 790E441483DE83FE CRC64;
MRIEFSPPDI TQLEIDEVVD TLKSGWITTG PKTKKLEQEL SVFTNTDKTV CLNSATAAME
LTLRLLGVGA GDEVITCAYT YTASASVIHH VGAKIVLVDC NKEDKFMDLD ALENAITEKT
KVIIPVDLAG KPCKYDEIFE IVERKKSLFK PNNKLQEKIG RVIVMADAAH SLGAVYKGKP
SGSIADFTCF SFHAVKNFTV AEGGSVTWNR NLGLNDDEVY REFQLLSLHG QSKDALSKTK
LGSWEYDIVA PNYKCNLTDI ASGIGLAQLK RYPSLLKRRF EIVERYNKGF EGTRIKPFIH
FEEDRKSCCH LYIVNIEGAS EEDRNEIIVK MAERGIATNV HYKPLPMHTA YKNLGFDIKD
YPNAFDNYKS EITLPLHTLL TDEQVDYIIE NLKALV
//
