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Database: UniProt
Entry: A0A0M9VIT9_9FLAO
LinkDB: A0A0M9VIT9_9FLAO
Original site: A0A0M9VIT9_9FLAO 
ID   A0A0M9VIT9_9FLAO        Unreviewed;       381 AA.
AC   A0A0M9VIT9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KOS07029.1};
GN   ORFNames=AM493_14045 {ECO:0000313|EMBL:KOS07029.1};
OS   Flavobacterium akiainvivens.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1202724 {ECO:0000313|EMBL:KOS07029.1, ECO:0000313|Proteomes:UP000037755};
RN   [1] {ECO:0000313|EMBL:KOS07029.1, ECO:0000313|Proteomes:UP000037755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IK-1 {ECO:0000313|EMBL:KOS07029.1,
RC   ECO:0000313|Proteomes:UP000037755};
RA   Wan X., Hou S., Saito J., Donachie S.;
RT   "Whole genome sequence of Flavobacterium akiainvivens IK-1T, from decaying
RT   Wikstroemia oahuensis, an endemic Hawaiian shrub.";
RL   Submitted (AUG-2015) 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|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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:KOS07029.1}.
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DR   EMBL; LIYD01000005; KOS07029.1; -; Genomic_DNA.
DR   RefSeq; WP_054408664.1; NZ_LIYD01000005.1.
DR   AlphaFoldDB; A0A0M9VIT9; -.
DR   STRING; 1202724.AM493_14045; -.
DR   PATRIC; fig|1202724.3.peg.2917; -.
DR   OrthoDB; 9803729at2; -.
DR   Proteomes; UP000037755; Unassembled WGS sequence.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037755}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         195
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   381 AA;  41491 MW;  58BDAED8BD3E125B CRC64;
     MKFNTKAIHG GQHHDPSTGA VMPPVYQTST FAQTSPGVHT GYEYSRAANP TRTALENALA
     SIENGTRGLA FSSGLAATDT VMKLLKPGDE VIAMDDLYGG TYRMFTRIYA DYGITFHFVD
     LNDTEKLKAL INDKTKLVWM ETPTNPLMKL ADISAVAEIT KSKNILFAVD NTFATPYLQR
     PLDLGADIVM HSATKYLGGH SDVIAGALVV RDESLGEKLH FAQFATGGTL GPQDSYLVLR
     GIKTLHIRME RHCLNGQKVA EYLAQHPKVA TVFYPGLESH PQHELAKRQM QGGFGGMVSF
     TFKSGEKADA ISFLENVKVF TLAESLGGVE SLANHPALMT HASIPEPKRK EIGITDDLVR
     LSVGIEDIDD LIEDIETALA P
//
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