ID   A0A1D8AU40_9BACT        Unreviewed;       477 AA.
AC   A0A1D8AU40;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AOS44403.1};
DE            EC=2.5.1.48 {ECO:0000313|EMBL:AOS44403.1};
GN   Name=metB {ECO:0000313|EMBL:AOS44403.1};
GN   ORFNames=Verru16b_01465 {ECO:0000313|EMBL:AOS44403.1};
OS   Lacunisphaera limnophila.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC   Lacunisphaera.
OX   NCBI_TaxID=1838286 {ECO:0000313|EMBL:AOS44403.1, ECO:0000313|Proteomes:UP000095228};
RN   [1] {ECO:0000313|EMBL:AOS44403.1, ECO:0000313|Proteomes:UP000095228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IG16b {ECO:0000313|EMBL:AOS44403.1,
RC   ECO:0000313|Proteomes:UP000095228};
RA   Rast P., Gloeckner I., Jogler M., Boedeker C., Jeske O., Wiegand S.,
RA   Reinhardt R., Schumann P., Rohde M., Spring S., Gloeckner F.O., Jogler C.;
RT   "Three novel species with peptidoglycan cell walls form the new genus
RT   Lacunisphaera gen. nov. in the family Opitutaceae of the verrucomicrobial
RT   subdivision 4.";
RL   Submitted (JUN-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|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CP016094; AOS44403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D8AU40; -.
DR   STRING; 1838286.Verru16b_01465; -.
DR   KEGG; obg:Verru16b_01465; -.
DR   PATRIC; fig|1838286.3.peg.1480; -.
DR   OrthoDB; 262490at2; -.
DR   Proteomes; UP000095228; Chromosome.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; PTHR42699; -; 1.
DR   PANTHER; PTHR42699:SF1; CYSTATHIONINE GAMMA-SYNTHASE-RELATED; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095228};
KW   Transferase {ECO:0000313|EMBL:AOS44403.1}.
SQ   SEQUENCE   477 AA;  51337 MW;  CA288DAFBC4F2E92 CRC64;
     MHAVRGYEEK DPAIVRQLTN GYPRFVLHPF TRRLVAHLTT VTPALRQRTL WLTSSGAMAQ
     ALLAHLTPAR GAELYTLPGL HGVSHPESPE TAALAKVFLQ NLGGFLSSRE AEDHLVALQL
     LPAPHPEEVF AGDAPAEIRR QLRTVLPGTT DADLLLASCG MSAMHAAFRA VNSLQAPRGR
     TVWLQLGWLY LDTIAILKKF TAHPADYVYV REVADLDALR RIFAAHGARI AGVVTEVPTN
     PLIQTPDLPA IAALCREHGA RLLVDPSMSS VFSLDVLPHA DLVVSSLTKY TASEGDLTAG
     LVAVNPAAPA AAALRSALAG TAEPLYARDA ARLAWQIGQT PAVLARIQAA TPSVVAFLEK
     HPAVKAVFWA LQSGSRENYL KLARTPDATG GMITFTLRNP GGLEKFYDRL RLPKGPSFGM
     KTTLICPFMY LAHYDLVTTP AGLAELAASR LDPDLLRLCV GTEPVDEIIR ALSEALA
//