ID   A8UIQ4_9FLAO            Unreviewed;       379 AA.
AC   A8UIQ4;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:EDP71056.1};
GN   ORFNames=FBALC1_01192 {ECO:0000313|EMBL:EDP71056.1};
OS   Flavobacteriales bacterium ALC-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP71056.1, ECO:0000313|Proteomes:UP000003630};
RN   [1] {ECO:0000313|EMBL:EDP71056.1, ECO:0000313|Proteomes:UP000003630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALC-1 {ECO:0000313|EMBL:EDP71056.1,
RC   ECO:0000313|Proteomes:UP000003630};
RA   Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) 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:EDP71056.1}.
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DR   EMBL; ABHI01000002; EDP71056.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8UIQ4; -.
DR   STRING; 391603.FBALC1_01192; -.
DR   eggNOG; COG0626; Bacteria.
DR   OrthoDB; 9803729at2; -.
DR   Proteomes; UP000003630; 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:UP000003630}.
FT   MOD_RES         195
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   379 AA;  41697 MW;  21AACE4BFB729E23 CRC64;
     MKFNTKTIHG GQEHDLAFGS VMPPIYQTST YAQSTPGGHK GYEYSRTHNP TRHALEKAFA
     SIENGNHGLA FASGLAAIDA ILKLLQSGDE VISTNDLYGG TYRLFTKIYE DFGIKFHFIG
     MENAEHIEDY INENTKLIWV ETPTNPMLNI IDIVTTAQIA KKHNVLLGVD NTFATPYLQQ
     PLDLGADIVM HSATKYLGGH SDLVMGALVV KDNGLAERLY FIQNASGAVC GPQDAFLALR
     GIKTLHIRMQ RHCENGKAVA TYLVNHPKIE NVYWPGLENH PNHEVAKSQM NDFGGMVSFT
     TKGNNYEEAI KIVENFKIFT LAESLGGVES LAGHPASMTH ASIPKENREK TGIVDSLIRL
     SVGIEDETDL IADLKQAID
//