ID   A0A136N0U2_9BACT        Unreviewed;       441 AA.
AC   A0A136N0U2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=OAH/OAS sulfhydrylase {ECO:0000313|EMBL:KXK39827.1};
GN   ORFNames=UZ09_BCD002000733 {ECO:0000313|EMBL:KXK39827.1};
OS   Bacteroidetes bacterium OLB9.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK39827.1, ECO:0000313|Proteomes:UP000070267};
RN   [1] {ECO:0000313|EMBL:KXK39827.1, ECO:0000313|Proteomes:UP000070267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB9 {ECO:0000313|EMBL:KXK39827.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-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:KXK39827.1}.
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DR   EMBL; LNBW01000022; KXK39827.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136N0U2; -.
DR   STRING; 1617420.UZ09_BCD002000733; -.
DR   PATRIC; fig|1617420.3.peg.781; -.
DR   Proteomes; UP000070267; Unassembled WGS sequence.
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   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; 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   NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   441 AA;  47835 MW;  89D856AB71AE589A CRC64;
     MSHFQTNALH AGYNPKSSKK SSSVPIYQTV SYVFDDVDYA AGVFNLSIPG YIYTRLNNPT
     NDILEQRLAA LEGGIGAVVT SSGTSAIATT LLTLLKSGDH IVASTSLYGG TFNLLHVTLP
     RFGITSSFVD PENPENFAQA ITPQTRAIFV ESLGNPRLDV LDLKAIAKIA HANKIPLIVD
     NTVASPYLLR PIEHGASIVI HSLTKYAAGN GTSLGGAIID AGTFDWSSGK FPEFTEPSPG
     YHGLVYHEAL GKAAFIAKIR IEGLRDLGAA LSPFNAFQII QGLETLPVRI EKHSENALKL
     AEWLEQRDEV AWVNYPGLKS SKYYTLAQKY LPNGQSGLLT FGLKKGYEAA KIIANNTQLF
     SLLANIGDTK SLIIHPASTT HQQLTEAEQK AAGVSPDLLR VSVGIEHIDD LKADLEQAFQ
     SLKNIQNESF EKHRDQALSY N
//