ID A0A2N6PKQ3_9MICO Unreviewed; 436 AA.
AC A0A2N6PKQ3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Bifunctional o-acetylhomoserine/o-acetylserine sulfhydrylase {ECO:0000313|EMBL:PMB99256.1};
GN ORFNames=CJ198_01595 {ECO:0000313|EMBL:PMB99256.1};
OS Brevibacterium luteolum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=199591 {ECO:0000313|EMBL:PMB99256.1, ECO:0000313|Proteomes:UP000235703};
RN [1] {ECO:0000313|EMBL:PMB99256.1, ECO:0000313|Proteomes:UP000235703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0680 {ECO:0000313|EMBL:PMB99256.1,
RC ECO:0000313|Proteomes:UP000235703};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
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:PMB99256.1}.
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DR EMBL; PNFZ01000001; PMB99256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6PKQ3; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000235703; 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:UP000235703}.
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 436 AA; 46103 MW; E5351BEEBB46DE27 CRC64;
MSELSFETRQ IHAGQSPDTA TGARALPIYQ TTSYVFDSAE TAANRFALAD LGPIYTRIGN
PTVAAVEDRI ADLEGGVQGL LVASGQSAEF LAIINIAEAG DHVVASPSLY GGTYNLLDVT
LRKLGIETTF VSDPGDVEAW KAAVKPNTKL FFAETVANPR SDVLDIAAVA TTAHAAGVPL
IIDNTLATPY LVRPIEHGAD VVIHSATKYL GGHGTSIAGI IVDSGNFDYS AEPERFPGFN
QPDASYNGLV YARDLGPDSP FGANVSYGIK ARVQLLRDLG PSASPFNAFL IAQGLETLSL
RIERHVANAQ RVAEFLESHA QVDKVHFAGL PSSPWYELGQ KYLPKGVGSV LGFEIADGYD
AAVKFVDALE LHSHVANIGD VRSLVIHPAS TTHSQLDEDA QRAAGVSPAF VRLAVGIEGI
DDIIADLEKG FAAARG
//