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Database: UniProt
Entry: Q3AAW1_CARHZ
LinkDB: Q3AAW1_CARHZ
Original site: Q3AAW1_CARHZ 
ID   Q3AAW1_CARHZ            Unreviewed;       421 AA.
AC   Q3AAW1;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   24-JAN-2024, entry version 95.
DE   SubName: Full=O-acetylhomoserine/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:ABB14069.1};
GN   OrderedLocusNames=CHY_1904 {ECO:0000313|EMBL:ABB14069.1};
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194 {ECO:0000313|EMBL:ABB14069.1, ECO:0000313|Proteomes:UP000002706};
RN   [1] {ECO:0000313|EMBL:ABB14069.1, ECO:0000313|Proteomes:UP000002706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901
RC   {ECO:0000313|Proteomes:UP000002706};
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Haft D.H., Nelson W.C.,
RA   Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B.,
RA   Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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; CP000141; ABB14069.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3AAW1; -.
DR   STRING; 246194.CHY_1904; -.
DR   KEGG; chy:CHY_1904; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_9; -.
DR   InParanoid; Q3AAW1; -.
DR   OMA; TYTLFAH; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000002706; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000002706}.
FT   MOD_RES         204
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   421 AA;  45632 MW;  7D4BE5E7AC4F1D4C CRC64;
     MKFATKALHA GQKPDRETRA RAVPIYQTTS YVFESTEHAA ALFNLEGGGY IYTRIDNPTT
     EVLENRIAAL EGGIGALAVA SGQAAITFAL LNLASAGDEI VASSNLYGGT YTLLANTFKS
     FGINVKFTEN VEVESFEKLI TPKTRALYVE TIGNPGLTIP DFEALSKLAQ SYKIPLVVDN
     TFATPYLFRP LEHGANIVIH SLTKFIGGHG VAIGGIIVDG GNFDWEAGGF TQFTTPDPAY
     HGMIYTEKFG AAAYIARART QFLRDIGASL SPFNAFLILL GVETLELRMK KHSENALKIA
     EYLKGHPKVT FVNYPGLSDH PHYNRAQKYF KNGFGAMLTF GVKGGREAGK KVIEGVKIFS
     HLANVGDAKS LIIHPASTTH SQLNSEELLK AGVTEDLIRL SIGIEDVDDL IQDLDNALAQ
     V
//
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