ID A0A085U165_9RHOB Unreviewed; 427 AA.
AC A0A085U165;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase/o-acetylserine sulfhydrylase {ECO:0000313|EMBL:KFE36712.1};
GN ORFNames=DW2_01100 {ECO:0000313|EMBL:KFE36712.1};
OS Thioclava atlantica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1317124 {ECO:0000313|EMBL:KFE36712.1, ECO:0000313|Proteomes:UP000028607};
RN [1] {ECO:0000313|Proteomes:UP000028607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13D2W-2 {ECO:0000313|Proteomes:UP000028607};
RA Lai Q., Li G., Shao Z.;
RT "Thioclava sp. 13D2W-2 Genome Sequencing.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFE36712.1, ECO:0000313|Proteomes:UP000028607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13D2W-2 {ECO:0000313|EMBL:KFE36712.1,
RC ECO:0000313|Proteomes:UP000028607};
RX PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT Ocean.";
RL Antonie Van Leeuwenhoek 107:297-304(2015).
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:KFE36712.1}.
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DR EMBL; AQRC01000001; KFE36712.1; -; Genomic_DNA.
DR RefSeq; WP_038142655.1; NZ_AQRC01000001.1.
DR AlphaFoldDB; A0A085U165; -.
DR STRING; 1317124.DW2_01100; -.
DR PATRIC; fig|1317124.6.peg.216; -.
DR eggNOG; COG2873; Bacteria.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000028607; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Transferase {ECO:0000313|EMBL:KFE36712.1}.
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 427 AA; 45419 MW; 2EA12786E2C8A052 CRC64;
MSDYKFDTLQ IHAGAVPDPA TGALQTPIYQ TTAYAFKDAE HAARLFNLEE VGFIYSRLTN
PTVMKLAERV AALEGGAGAV CCSSGHAAQI MALFPLMAPG CNIIASTRLY GGTITQFSQT
IKRFGWSCTF VDFDDLEALE AAVDENTRAI FCESISNPGG YITDIPAVAK LTDKLGLPLI
VDNTLATPYL CRPIEMGATL VVHSLTKYMT GNGTVTGGCV VDSGKFDWSA SGKFPSLSEP
EPAYHGLRFH EALGPMAFTF HSIAVGLRDL GMTMNPQGAH YTLLGIETLS LRMAKHVANA
KAVADWLEAD PRIDFVTYAG LESSPWHDRM KSVCPRGAGG LFTVAVKGGY EACVKLVDSL
ALFSHVANLG DARSLIIHSA STTHRQLTEA QQIAAGAAPN VVRLSIGIED AGDLIADLDQ
ALAIATA
//
