ID   Q3B0Q7_SYNS9            Unreviewed;       427 AA.
AC   Q3B0Q7;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Spore coat polysaccharide biosynthesis protein spsC {ECO:0000313|EMBL:ABB25071.1};
GN   OrderedLocusNames=Syncc9902_0096 {ECO:0000313|EMBL:ABB25071.1};
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB25071.1, ECO:0000313|Proteomes:UP000002712};
RN   [1] {ECO:0000313|Proteomes:UP000002712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000097; ABB25071.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3B0Q7; -.
DR   STRING; 316279.Syncc9902_0096; -.
DR   KEGG; sye:Syncc9902_0096; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_7_1_3; -.
DR   Proteomes; UP000002712; Chromosome.
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:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 2.
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        210
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   427 AA;  47297 MW;  9E67F3180AEDAB8C CRC64;
     MNNSSELAIN GGSPIITPSH SFLPYNTIGH EEKCAVNDVL KSGNLSGFVA SSGKQFFGGP
     QVQLFENDLR TFFNVKHAIT VNSWTSGLIV MLGALGLEPG DEVITTPWTM CATATAILHW
     NAIPIFADIN SKTFLLDLDL VESLISTRTK AILAVDIFGQ SCDMDKLKYL QDKYNVFIVS
     DSAQAPYAQQ NQRFAGTLGD CGGFSFNYHK HIHTGEGGAI VTNNSEIALR CQLIRNHAEA
     AVESMNIHNL SNMIGYNFRL GEMESAIGIQ QLKKLPSLVK NRQLIASRLI DGLRNLKGLI
     LPELLDSNTH VFYILPLSLE LSMLSCTRSD LVEALRFEGV PGLEEGYCNI HLLPLFQQRI
     AYGSKGFPWS SPDICSHVPN YEKGLCPVAE YLHDSSFFMI ELCLYSFTDY DVDLIIEAFH
     KVWSNLT
//