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Database: UniProt
Entry: F4XQB2_9CYAN
LinkDB: F4XQB2_9CYAN
Original site: F4XQB2_9CYAN 
ID   F4XQB2_9CYAN            Unreviewed;       321 AA.
AC   F4XQB2;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Putative pyridoxal phosphate-dependent, cell-wall biogenesis regulatory protein {ECO:0000313|EMBL:EGJ33226.1};
DE   Flags: Fragment;
GN   ORFNames=LYNGBM3L_41780 {ECO:0000313|EMBL:EGJ33226.1};
OS   Moorena producens 3L.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Moorena.
OX   NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ33226.1, ECO:0000313|Proteomes:UP000003959};
RN   [1] {ECO:0000313|Proteomes:UP000003959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX   PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA   Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA   Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA   Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA   Gerwick W.H., Gerwick L.;
RT   "Genomic insights into the physiology and ecology of the marine filamentous
RT   cyanobacterium Lyngbya majuscula.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
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}.
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DR   EMBL; GL890856; EGJ33226.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4XQB2; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_864695_0_0_3; -.
DR   OrthoDB; 9810913at2; -.
DR   Proteomes; UP000003959; Unassembled WGS sequence.
DR   CDD; cd00616; AHBA_syn; 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   PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000390-2}.
FT   ACT_SITE        132
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         132
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGJ33226.1"
SQ   SEQUENCE   321 AA;  35931 MW;  16B6D23A10F4BF70 CRC64;
     LTSSCHGALH LVLKAIGVEK GDEVIVPDIT WASGTVFPVC WVGAKPIFVD VKQDTWCIDP
     SLIEAKITSK TKAIIAVHLY GNMADMDELR TIANRHNLIL IEDAAEAIGS AYKGMKAGTI
     GDFGVFSFHG TKTVTTGEGG VIITNSDKYT ETLSTLENQG RKPGSRLFWC EEIGLKYKMS
     NIQAALGLAQ FERVEELVQK KRWIFEAYKN QLSDLPDKTM NHEDIHVTNG FWQPTIVFGD
     SWAFDEGRRN QLVDDMIAEK VQIRPFFYPV SSMPPFESNA NDENEISYSI YKTGINLPSY
     HELESEDISY IVQKLKNHLS S
//
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