ID Q5QY89_IDILO Unreviewed; 422 AA.
AC Q5QY89;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:AAV82846.1};
GN OrderedLocusNames=IL2014 {ECO:0000313|EMBL:AAV82846.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV82846.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV82846.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV82846.1; -; Genomic_DNA.
DR RefSeq; WP_011235242.1; NC_006512.1.
DR AlphaFoldDB; Q5QY89; -.
DR STRING; 283942.IL2014; -.
DR KEGG; ilo:IL2014; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_2_6; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000001171; 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.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 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:UP000001171}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 422 AA; 45628 MW; 125696E58EFF9A03 CRC64;
MKDETLAIHH GYETDPTTKS VATPIYQTVS YEFDNAQHGA DLFDLAVEGN IYTRIMNPTN
DVLEKRVAEL EHGVAALAVA SGMAAIEYAL ITLARQGDNI VTTPQLYGGT YTLFQHMLPS
FGIEVRFAES DKAEDIGKLI DGKTKAVFCE SIGNPAGNIA DLEGYAEVAH QHGVPLVVDN
TVATPILCKP IDFGADIVVH SLTKYIGGHG NSVGGLIVDS GGFDWVKQKQ RFPQFSSPEP
AYHGVVYTDA FGPAAFIARV RTVALRNTGA CLSPFNAFLL LQGLETLPLR IERHCENALK
VAEYLQSHPS VDWVNFAALP EHTNYERAKK YIKNGVPASL LTFGVKGGYD AGVEFYDKLK
LFKRLVNIGD AKSLACHPAS TTHRQLSAGE QAAVGVKPEA IRLCVGIENA EDIIADISQA
LA
//
