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Database: UniProt
Entry: A0A1V1ZI00_9FLAO
LinkDB: A0A1V1ZI00_9FLAO
Original site: A0A1V1ZI00_9FLAO 
ID   A0A1V1ZI00_9FLAO        Unreviewed;       456 AA.
AC   A0A1V1ZI00;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Cysteine synthase {ECO:0000313|EMBL:OMP31740.1};
GN   ORFNames=BKM32_01360 {ECO:0000313|EMBL:OMP31740.1};
OS   Mangrovimonas sp. DI 80.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mangrovimonas.
OX   NCBI_TaxID=1779330 {ECO:0000313|EMBL:OMP31740.1, ECO:0000313|Proteomes:UP000188854};
RN   [1] {ECO:0000313|EMBL:OMP31740.1, ECO:0000313|Proteomes:UP000188854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI 80 {ECO:0000313|EMBL:OMP31740.1,
RC   ECO:0000313|Proteomes:UP000188854};
RA   Krishnamurthi S., Pal Y., Verma A., Sundharam S.;
RT   "Taxonomic characterization of strain DI 80 closely related to
RT   Mangrovimonas sp.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:OMP31740.1}.
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DR   EMBL; MSDT01000002; OMP31740.1; -; Genomic_DNA.
DR   RefSeq; WP_076662228.1; NZ_MSDT01000002.1.
DR   AlphaFoldDB; A0A1V1ZI00; -.
DR   Proteomes; UP000188854; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
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   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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:UP000188854}.
FT   MOD_RES         285
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   456 AA;  51111 MW;  E38759C2A67D2396 CRC64;
     MEKDLKLFNE LAQILLEEEQ SQPVAKPIDT EQLYDSLDLE LPDEPTSEED FKASLLEIIK
     YTPKTASSSF FNQLYGGRVE KATLGDLLAV MLNTSMYTYK IGGPQIGIEK IILKKICEMI
     GYGPSSDGTF APGGSMSNFM AMVMARDKHS KTAPNKGVTS KMIVYTSEVS HYSINKNAAL
     MGIGRNQVRE VKTNDHGEML PEDLEMKIKQ DLAEGHHPFF VNCTAGTTVM GAFDDVTEIH
     KVSSKYNLWL HLDGAYCGSV IFSKKYAHLV KGIELTDSFS VNAHKMLGTP LSCSIIVTQN
     AEDLHISFSS EAEYLYQTDG DDYNLGKTSL QCGRRNDALK FWTLWKSIGT QGLETIVDKQ
     FQLADVARNY VSSHPDYTLY SFDNSISVCF NYKKTPAKQL CTALYENAKL MVSYGTFKGQ
     EFVRLVTINS ILEEKDIMNF FAELETFVQN NNFNPK
//
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