ID K6YTY1_9ALTE Unreviewed; 412 AA.
AC K6YTY1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:GAC20173.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:GAC20173.1};
GN Name=metY {ECO:0000313|EMBL:GAC20173.1};
GN ORFNames=GARC_3214 {ECO:0000313|EMBL:GAC20173.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC20173.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC20173.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC20173.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(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}.
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:GAC20173.1}.
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DR EMBL; BAEO01000047; GAC20173.1; -; Genomic_DNA.
DR RefSeq; WP_007621817.1; NZ_BAEO01000047.1.
DR AlphaFoldDB; K6YTY1; -.
DR STRING; 493475.GARC_3214; -.
DR eggNOG; COG2873; Bacteria.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000006327; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:GAC20173.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006327};
KW Transferase {ECO:0000313|EMBL:GAC20173.1}.
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 412 AA; 44721 MW; 9DE8D597E05E7F5C CRC64;
MKSKGFTSRL VHADRLLNTP ESGAVHQATN NSVLFEYKDA QELVDVFQGK KAGHVYSRSS
SGSNVALQNI LTHLEGGLGA ITFASGMAAI TATMFSLFKA GDHLIVSHFL FGNTRSFTET
MQSLGIELSF VDVTDVQNVK AAFKTNTKAV YLETIANPVT QVADLRAIGQ LCESKKTLFL
IDNTMTPANI FDANSVLASL TISSLTKYIA GHGNVLGGAV VDTGLFDWSS FENILPMYRG
PDKAQWGLTQ IRKRGLRDMG GTLSADSAHA ISIGLETLVL RTDKVCENAL RLASYLHSHN
KVSAVYYPGL AGHPQHYLAR EHFNGYGGIL SLDLADDIDP IQFLNALNLV ICATHLGDTR
TLALPVASTI YFECSAQQRQ DMGVSDNMIR MSIGIEDIDD IVADFEQAFA QF
//
