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Database: UniProt
Entry: A0A2N6PKQ3_9MICO
LinkDB: A0A2N6PKQ3_9MICO
Original site: A0A2N6PKQ3_9MICO 
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
//
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