ID I3ZA08_BELBD Unreviewed; 435 AA.
AC I3ZA08;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:AFL86076.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:AFL86076.1};
GN OrderedLocusNames=Belba_3578 {ECO:0000313|EMBL:AFL86076.1};
OS Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL86076.1, ECO:0000313|Proteomes:UP000006050};
RN [1] {ECO:0000313|Proteomes:UP000006050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC {ECO:0000313|Proteomes:UP000006050};
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Belliella baltica DSM 15883.";
RL Submitted (JUN-2012) 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; CP003281; AFL86076.1; -; Genomic_DNA.
DR RefSeq; WP_014774010.1; NC_018010.1.
DR AlphaFoldDB; I3ZA08; -.
DR STRING; 866536.Belba_3578; -.
DR KEGG; bbd:Belba_3578; -.
DR PATRIC; fig|866536.3.peg.3708; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_10; -.
DR OrthoDB; 9803729at2; -.
DR Proteomes; UP000006050; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000006050};
KW Transferase {ECO:0000313|EMBL:AFL86076.1}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 435 AA; 47202 MW; 9CA4C9E63F1A4836 CRC64;
MSSNYRFDTL QLHAGQSPDS ATNSRAVPIY QTTSYVFNSA EHGANLFALK EFGNIYTRIM
NPTTDVFEQR VAALEGGVAA VATGSGQAAQ FLALNNILQT GENFVSTSFL YGGSYNQFKV
AFKRIGIEAR FAKGNNPEDF EKLIDNKTKA LYLETIGNPE FNIPDFEAIA AVAKKRGIPL
VVDNTFGAGG FLFAPIKHGA NIVTASATKW IGGHGTSVGG IIVDGGNFNW GNGKFPQFTE
PSEGYHGLKF WEVFGENNPL GLPNIAFVIR ARVEGLRDFG PALSPFNSFL LLQGLETLSL
RVQRTVGNAL AIAEWLESHP QVQKVNYPGL KSSPYHALAT KYLTNGFGGV LSFEIKGDKE
STSDFINKLE LISHLANVGD AKTLIIQPSA TTHQQLSDEE QKAAGVTPTL LRLSLGIEHI
EDIKADLQQA FDHVK
//
