ID E3CWI0_9BACT Unreviewed; 429 AA.
AC E3CWI0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=O-acetylhomoserine sulfhydrolase {ECO:0000313|EMBL:EFQ24335.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:EFQ24335.1};
GN ORFNames=Apau_1921 {ECO:0000313|EMBL:EFQ24335.1};
OS Aminomonas paucivorans DSM 12260.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Aminomonas.
OX NCBI_TaxID=584708 {ECO:0000313|EMBL:EFQ24335.1, ECO:0000313|Proteomes:UP000005096};
RN [1] {ECO:0000313|EMBL:EFQ24335.1, ECO:0000313|Proteomes:UP000005096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12260 {ECO:0000313|EMBL:EFQ24335.1,
RC ECO:0000313|Proteomes:UP000005096};
RX PubMed=21304733;
RA Pitluck S., Yasawong M., Held B., Lapidus A., Nolan M., Copeland A.,
RA Lucas S., Del Rio T.G., Tice H., Cheng J.F., Chertkov O., Goodwin L.,
RA Tapia R., Han C., Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Pukall R., Spring S., Rohde M., Sikorski J., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Non-contiguous finished genome sequence of Aminomonas paucivorans type
RT strain (GLU-3).";
RL Stand. Genomic Sci. 3:285-293(2010).
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; CM001022; EFQ24335.1; -; Genomic_DNA.
DR RefSeq; WP_006301571.1; NZ_CM001022.1.
DR AlphaFoldDB; E3CWI0; -.
DR STRING; 584708.Apau_1921; -.
DR PaxDb; 584708-Apau_1921; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_0; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000005096; Chromosome.
DR GO; GO:0016787; F:hydrolase 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 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 Hydrolase {ECO:0000313|EMBL:EFQ24335.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000005096};
KW Transferase {ECO:0000313|EMBL:EFQ24335.1}.
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 429 AA; 46239 MW; 0E12BF565766A5F7 CRC64;
MTNRTKQGLA TRALHAGWRS DPATGAFGLP IYLTAAYQFR DSEHAVRLFE LEEEGHLYSR
LSNPTVAAYE AAVADLEGGV GALATSSGQA AFTHLLAALC SAGDHLVVSR KLYGGTLTLV
KNTFARFGVT HTLVDTDEPD QVEGACTPAT RAILTETVGN PALNVAPLEE LGRIARARDA
VLVVDNTFPT PCLCRPIEWG AHVVVHSTTK FLSGQGNVIG GMVVDGGTMD WKASGRWPLL
TQPDPSYHGV VFSDRFGPAA LAAKLRATLL RDLGGTPSAF DSYLLRQSLG TLPLRMARHS
ENALTVARYL QDHRQIDWVR YPGLDSHPQR ERAKRYLPDG CGGMVACGIR GGVEAGRRFL
DALELFGHMA NLGDSRSLAI HPASTTHSQL TREERLAGGI EDGLIRLSVG LEDPRDLVED
LDRAFSAAR
//