ID   A0A0A1FG99_9BURK        Unreviewed;       428 AA.
AC   A0A0A1FG99;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:AIY41897.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:AIY41897.1};
GN   ORFNames=LT85_2739 {ECO:0000313|EMBL:AIY41897.1};
OS   Collimonas arenae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279058 {ECO:0000313|EMBL:AIY41897.1, ECO:0000313|Proteomes:UP000030302};
RN   [1] {ECO:0000313|EMBL:AIY41897.1, ECO:0000313|Proteomes:UP000030302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cal35 {ECO:0000313|EMBL:AIY41897.1,
RC   ECO:0000313|Proteomes:UP000030302};
RA   Uroz S., Tech J.J., Sawaya N.A., Frey-Klett P., Leveau J.H.J.;
RT   "Structure and function of bacterial communities in ageing soils: insights
RT   from the Mendocino ecological staircase.";
RL   Soil Biol. Biochem. 69:265-274(2014).
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; CP009962; AIY41897.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1FG99; -.
DR   STRING; 279058.LT85_2739; -.
DR   KEGG; care:LT85_2739; -.
DR   HOGENOM; CLU_018986_4_0_4; -.
DR   Proteomes; UP000030302; Chromosome.
DR   GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Transferase {ECO:0000313|EMBL:AIY41897.1}.
FT   MOD_RES         224
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   428 AA;  46385 MW;  A8A75E5F191E6E98 CRC64;
     MLFAFFVDKK AFKQSANMTQ KYGFTTTILH SDRQKTIEHG APHKPVHTSV TWGYSDARQL
     AEVFQGKQSG YRYGRQGNPT VAALEDKVTK MEGGLASICF ASGMAAIGAL IQALLREGDH
     VVSSVFLFGN TASMWQTFGG QGGKVSMVDA TDVANVEAAL TPATRMVFVE TIANPRTQVA
     DLKRIGELCR ARGILFVVDN TMTSPYLFQP KTVGAGLVVN SLTKSIGGHG NALGGALTDT
     GLFDWSSFPN IYDAYKRNPP VQWALAQIRA KSLRDFGASL GPEAAHHIAV GAETIALRME
     RSSASALAVA RMLEADPRVA AVHYPGLESH PQYVLAGELF RSSSYLFSFE LKPEIDCFDY
     LNRLKLAISG THLGDNRTLV IAVAHTIFYE IGAERRAAMG IGESLIRVSI GIEDTTDLVE
     DFRQALQA
//