ID L0I8C4_HALRX Unreviewed; 475 AA.
AC L0I8C4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=OAH/OAS sulfhydrylase {ECO:0000313|EMBL:AGB15058.1};
GN OrderedLocusNames=Halru_0416 {ECO:0000313|EMBL:AGB15058.1};
OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halovivax.
OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB15058.1, ECO:0000313|Proteomes:UP000010846};
RN [1] {ECO:0000313|Proteomes:UP000010846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18193 / JCM 13892 / XH-70
RC {ECO:0000313|Proteomes:UP000010846};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Halovivax ruber XH-70.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|ARBA:ARBA00009077}.
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DR EMBL; CP003050; AGB15058.1; -; Genomic_DNA.
DR AlphaFoldDB; L0I8C4; -.
DR STRING; 797302.Halru_0416; -.
DR KEGG; hru:Halru_0416; -.
DR eggNOG; arCOG00061; Archaea.
DR HOGENOM; CLU_018986_4_0_2; -.
DR OrthoDB; 43458at2157; -.
DR Proteomes; UP000010846; 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 Reference proteome {ECO:0000313|Proteomes:UP000010846}.
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 50526 MW; A2BD07F2548A9D3F CRC64;
MRDEGDLPRS DDGWSTPRDG QAKEGTQANS NRSADRNRRT ALATRSLHGG YRPDPGTGAA
ATPIVQSTSY EFVDADDAAA RYALERDDYI YSRIANPTVD TLETRLAELA GGTGAVATGS
GMAALDAITL PLAGVGDNVV CSTDTYGGTT AYFRSTAARR GIEPRFVPTL DTDAYADAID
AETAFVHVET IGNPSLVTPD FEAISSIAHD HGVPLVVDNT FATPALCRPI AHGADIVWAS
TTKWLHGHGT TLGGILIDGG SFPWRDHADR YPELAGENPA YADVDFGRDF AEAPFAAAAR
FRSLRSLGNG QSPVDAWQTL QGLETLPLRM ARHCENAAIV ADYLADHDDV AWVSYPGLDS
HETHDTARRY LDDFGGMFAF GLVAGDDASP SAFEAGKRFC ESVELASFLA NVGDAKTLVI
HPASTTHGQL TPDERADAGV SEELVRVSVG IEDPADLLAD FEQAIERATS ASPRP
//
