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Database: UniProt
Entry: A0A1H3LUS4_9MICO
LinkDB: A0A1H3LUS4_9MICO
Original site: A0A1H3LUS4_9MICO 
ID   A0A1H3LUS4_9MICO        Unreviewed;       456 AA.
AC   A0A1H3LUS4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:SDY68152.1};
GN   ORFNames=SAMN05216554_1143 {ECO:0000313|EMBL:SDY68152.1};
OS   Herbiconiux ginsengi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Herbiconiux.
OX   NCBI_TaxID=381665 {ECO:0000313|EMBL:SDY68152.1, ECO:0000313|Proteomes:UP000198891};
RN   [1] {ECO:0000313|EMBL:SDY68152.1, ECO:0000313|Proteomes:UP000198891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3491 {ECO:0000313|EMBL:SDY68152.1,
RC   ECO:0000313|Proteomes:UP000198891};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNPZ01000001; SDY68152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3LUS4; -.
DR   STRING; 381665.SAMN05216554_1143; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000198891; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase 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   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   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   Lyase {ECO:0000313|EMBL:SDY68152.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198891}.
FT   MOD_RES         215
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   456 AA;  48342 MW;  D64A86C60F0A6A03 CRC64;
     MTEESTRDRE FGFATQQVHA GAFTDDGVNA RATPIYLSAG FVFDDFAQAR DRFGGVDDGF
     SYTRVGNPTT ASVERRIAAL EHGEQAILVG SGQAALSVAL LGLLQAGDHL VSASSIYEGS
     RGLFLDNFSR LGIDTSFVID ANDPLAWELA IRPTTRALFV ESIPNPRNDI VDLALVAAVA
     HRHGIPLIVD NTFATPYLLR PLEHGADVVV HSASKFLAGH GAVLGGVIVS GSGFDWAARP
     ELFPHLTEPA RALGGRSYAE RFGSSAFITY ARDVVALRFG PTPSPLNAFL IQQGIETLSL
     RVDRQSSSAQ AVAEWLEAQP EIESVDYSGL PSNPYNELAR RYLPRGQGSV FSFTVAGGLA
     AAEALIDAVA LFTRMTHLGD VRSLIIHPGT TSHALRTAEQ LREGGIGPGL IRLSIGVEDV
     ADLIADLAQA LDAVRSLDAG RPATVAETAG FAGSGR
//
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