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
//