ID A0A139X1M0_9CYAN Unreviewed; 458 AA.
AC A0A139X1M0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:KYC38609.1};
GN ORFNames=WA1_36115 {ECO:0000313|EMBL:KYC38609.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC38609.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC38609.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC38609.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYC38609.1}.
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DR EMBL; ANNX02000040; KYC38609.1; -; Genomic_DNA.
DR RefSeq; WP_017745774.1; NZ_KQ976354.1.
DR AlphaFoldDB; A0A139X1M0; -.
DR STRING; 128403.WA1_36115; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF4; TYROSINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925}.
FT MOD_RES 259
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 458 AA; 51080 MW; 2493D89F3FEFA3AF CRC64;
MILEKESLGL LQEALARLEE GFHNLPKCDL SPNLDALRLI LLEVADRMQD NYPYPHPLYA
GQMLKPPTEI ARLAYTLSLW INPNNHALDG GRASSAMERE AVAEIAKMFG WETHLGHLCS
GGTMANLEGL WVAENLQPNK KVVASNQAHY THSRICGVLR LPFQSVPCDS HARMDVAALK
KLLQEDDIGT VVVTIGTTAT GSIDPLPEIL ELQAEYEFRI HVDTAYGGYF TLIDNLDTET
KAAFDCLKRV DSIVVDPHKH GLQPYGCGCI LFKDPSIGKL YKHDSPYTYF SSEELHLGEI
SLECSRPGSS AVALWATQRL LPLIRGGQFA ASLSQSRKAA LTLFEKLQND SRFIVIFPPQ
LDIVVWVVKS QSASESSRLA KEIFEAAARE NLHLAIANLP KELLLETGEE INWDRDSITC
LRSCLMKPEH LDWIDHIWQI LNSVTNKVLQ TGEFKRAS
//
