ID M0F205_9EURY Unreviewed; 401 AA.
AC M0F205;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Cys/Met metabolism pyridoxal-phosphate-dependent protein {ECO:0000313|EMBL:ELZ54086.1};
GN ORFNames=C467_12113 {ECO:0000313|EMBL:ELZ54086.1};
OS Halorubrum hochstenium ATCC 700873.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227481 {ECO:0000313|EMBL:ELZ54086.1, ECO:0000313|Proteomes:UP000011689};
RN [1] {ECO:0000313|EMBL:ELZ54086.1, ECO:0000313|Proteomes:UP000011689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700873 {ECO:0000313|EMBL:ELZ54086.1,
RC ECO:0000313|Proteomes:UP000011689};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELZ54086.1}.
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DR EMBL; AOJO01000055; ELZ54086.1; -; Genomic_DNA.
DR RefSeq; WP_008585605.1; NZ_AOJO01000055.1.
DR AlphaFoldDB; M0F205; -.
DR STRING; 1227481.C467_12113; -.
DR GeneID; 72714428; -.
DR PATRIC; fig|1227481.4.peg.2393; -.
DR OrthoDB; 43458at2157; -.
DR Proteomes; UP000011689; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 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 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000011689}.
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43294 MW; 2EF232342C0BFA7A CRC64;
MSDRSDESDR AGDGDSADDR RFETRAIHAG QEPDPETGAL MTPIHANSTY EQDGPGEHRG
YEYSRTGNPT RTDLEANLAS LESGSHARCF SSGMGAINTV LNLLSAGDHV VAGDDVYGGT
HRILTQVYDE YDIETTFVDT TDHDAVREAV REETELVWVE TPTNPLMNVN DIGALADIAH
EADALCAVDN TFATPYLQRP LEHGADIVSQ SLTKYLGGHS DTIGGALIVD DAELDERLGF
YQNSVGATPG PFDAFLVLRG TKTLPVRMDR HCENAMALAE WLEGHDAVER VYYPGLESHP
DHELAAEQMD DFGGMLSFEL DGTLEEASTV VSETEVFTLA ESLGGVESLI EQPAAMTHAA
IPREERLAAG LTDGLVRVSV GIEHVDDMKA DLQAAFDAAL S
//
