ID A0A2S8WR31_9MICC Unreviewed; 448 AA.
AC A0A2S8WR31;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Bifunctional o-acetylhomoserine/o-acetylserine sulfhydrylase {ECO:0000313|EMBL:PQZ93002.1};
GN ORFNames=CQ018_11135 {ECO:0000313|EMBL:PQZ93002.1};
OS Arthrobacter sp. MYb227.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1848601 {ECO:0000313|EMBL:PQZ93002.1, ECO:0000313|Proteomes:UP000239972};
RN [1] {ECO:0000313|EMBL:PQZ93002.1, ECO:0000313|Proteomes:UP000239972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb227 {ECO:0000313|EMBL:PQZ93002.1,
RC ECO:0000313|Proteomes:UP000239972};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) 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:PQZ93002.1}.
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DR EMBL; PCPT01000004; PQZ93002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8WR31; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000239972; 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.
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:UP000239972}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 448 AA; 47338 MW; 0BED9F07EC76BE1A CRC64;
MSNDWSFETR QIHVGQEPDA TTGARALPIY QTTAFVFPSA ESAANRFALS DLGPIYTRIG
NPTQGAVEDR IANLEGGVGA LLLASGQAAT TFSILNLAEA GDHIVASPSL YGGTQNLFKH
TLRKLGIEVT FVADPDDLEG WKAAIKPNTK AFFGEVVSNP RQDVLDIEGI SGIAHEAGVP
LIVDNTLSTP YLIRPIEWGA DIVVHSATKY LGGHGTASAG VIVDSGNFDF AASPEKFPGF
NTPDESYNGL VFARDLGVNG ILGANLAYVL KARVQLLRDL GSAIAPFNAF LIAQGLETLS
LRMERHVSNA VVVAKWLETQ EQVKSVTYAG LESSPWFERG RKYGPQGTGA IVSFEISGGR
EAGQGFVDAL KLHSHVANLG DVRSLVVHPA STTHSQLTEA EQVAAGVSPG LVRLSVGIEN
VVDIIADLQA GFEAVASLAE GELQGVAR
//
