ID B2IST7_STRPS Unreviewed; 417 AA.
AC B2IST7;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Capsular polysaccharide biosynthesis protein, putative {ECO:0000313|EMBL:ACB91064.1};
GN OrderedLocusNames=SPCG_1812 {ECO:0000313|EMBL:ACB91064.1};
OS Streptococcus pneumoniae (strain CGSP14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=516950 {ECO:0000313|EMBL:ACB91064.1, ECO:0000313|Proteomes:UP000001682};
RN [1] {ECO:0000313|EMBL:ACB91064.1, ECO:0000313|Proteomes:UP000001682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGSP14 {ECO:0000313|EMBL:ACB91064.1,
RC ECO:0000313|Proteomes:UP000001682};
RX PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT "Genome evolution driven by host adaptations results in a more virulent and
RT antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL BMC Genomics 10:158-158(2009).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP001033; ACB91064.1; -; Genomic_DNA.
DR AlphaFoldDB; B2IST7; -.
DR KEGG; spw:SPCG_1812; -.
DR HOGENOM; CLU_033332_0_3_9; -.
DR Proteomes; UP000001682; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 417 AA; 46667 MW; 056757BCF1DDEE68 CRC64;
MSTDKRSKSM PNYNIPFSPP DITEAEIAEV ADTLRSGWIT TGPKTKELER RLSLYTQTPK
IVCLNSATAA LELILRVLEV GPGDEVIVPA MTYTASCSVI THVGATPVMV DIQADTFEMD
YDLLEQAITE KTKVIIPVEL AGIVCDYDRL FQVVEKKRDF FTASSKWQKA FNRIVIVSDS
AHALGSTYKG QPSGSIADFT SFSFHAVKNF TTAEGGSATW RANPVIDDEE MYKEFQILSL
HGQTKDALAK MQLGSWEYDI VTPAYKCNMT DIMASLGLVQ LDRYPSLLQR RKDIVDRYDS
GFAGSRIHPL AHKTETVESS RHLYITRVEG ASLEERNLII QELAKAGIAS NVHYKPLPLL
TAYKNLGFDM TNYPKAYAFF ENEITLPLHT KLSDEEVDYI IETFKTVSEK VLTLSKK
//
