GenomeNet

Database: UniProt
Entry: A0A0G1GYM7_9BACT
LinkDB: A0A0G1GYM7_9BACT
Original site: A0A0G1GYM7_9BACT 
ID   A0A0G1GYM7_9BACT        Unreviewed;       410 AA.
AC   A0A0G1GYM7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=O-acetylhomoserine sulfhydrolase {ECO:0000313|EMBL:KKT40216.1};
GN   ORFNames=UW30_C0023G0014 {ECO:0000313|EMBL:KKT40216.1};
OS   Candidatus Giovannonibacteria bacterium GW2011_GWA2_44_13b.
OC   Bacteria; Candidatus Giovannonibacteria.
OX   NCBI_TaxID=1618647 {ECO:0000313|EMBL:KKT40216.1, ECO:0000313|Proteomes:UP000034736};
RN   [1] {ECO:0000313|EMBL:KKT40216.1, ECO:0000313|Proteomes:UP000034736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKT40216.1}.
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; LCHU01000023; KKT40216.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1GYM7; -.
DR   STRING; 1618647.UW30_C0023G0014; -.
DR   Proteomes; UP000034736; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR   PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KKT40216.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         227
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   410 AA;  45370 MW;  FC61A4A8ADCF3811 CRC64;
     MAKRKSAKEH KLHAKTLEIH GGGSLYDTEL RIGVDRVTAY PLGSVARGTK LFAGEEDGFV
     YSRINNRTVD KLERRLASME GAEACLATSS GMSAITLLSL YLARTRDNRK GGIVSSNRLY
     GGVFHLFHEI LLRLGIDVSF VDDPHDIYNW EYANYWHKIG LDPPRALRFF HLENPSNPLI
     DVFDVGTIAE VAHKFEVPLV VDSTLATPAL LKPLELGADF VVHSLSKYMG DGEVIGGAIL
     GKKDVIDDLK KTWFRDMGPC MSPDNAAIFL SHVESLSVRM TEHCRNAEKV AKFLSRHEKV
     KQVFYPSVGV RSKRNKSLMT KGFGGLMAFE VKGGVKAATK VIENLKLFWH APNIGESRSL
     VLIPWLTTHG LMSDKDKSKA GILPGVIRAS LGREDDRDLC EDLGQALAKI
//
DBGET integrated database retrieval system