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}.
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; 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
//