ID E3I4T0_RHOVT Unreviewed; 449 AA.
AC E3I4T0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Cysteine synthase {ECO:0000313|EMBL:ADP72752.1};
DE EC=2.5.1.47 {ECO:0000313|EMBL:ADP72752.1};
GN OrderedLocusNames=Rvan_3579 {ECO:0000313|EMBL:ADP72752.1};
OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS 4299).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Rhodomicrobium.
OX NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP72752.1, ECO:0000313|Proteomes:UP000001399};
RN [1] {ECO:0000313|Proteomes:UP000001399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC {ECO:0000313|Proteomes:UP000001399};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR EMBL; CP002292; ADP72752.1; -; Genomic_DNA.
DR AlphaFoldDB; E3I4T0; -.
DR STRING; 648757.Rvan_3579; -.
DR KEGG; rva:Rvan_3579; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_2_5; -.
DR OMA; DEAWVNT; -.
DR Proteomes; UP000001399; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; 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; IPR004841; AA-permease/SLC12A_dom.
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 PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR PANTHER; PTHR43797:SF2; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR Pfam; PF00324; AA_permease; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000001399};
KW Transferase {ECO:0000313|EMBL:ADP72752.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..115
FT /note="Amino acid permease/ SLC12A"
FT /evidence="ECO:0000259|Pfam:PF00324"
SQ SEQUENCE 449 AA; 48193 MW; D3C500418AF49548 CRC64;
MIVTVLSVGL FFVFTGYVLV AAFQGAATGL DKVDAPLSVL ATSVGLEPLG LLIAAGVAAS
FFASALGSIN AGARIIYSLS RHGIIFGRAG DAHETHATPH VAVAISAAIA ALLALPLHEI
VAAKTLYGGS FNLFQNTLPK HGVRTTLVDP ADTDNFERAI NERTRALFVE TIGNPDINII
DFEAVARIAE RHGIPLIVDN TFATPYLFRP FDYGANISVH SATKFIGGHG TSIGGLIVDG
GNFNWANGKF PDFTTPDPAY SGFVHWDKWG NYPGVGNIAY IIKARLHYLR DLGASLSPFN
AFLFLQGLET LSFRLERQIA NAQAIAEWLE ANPEVEWVNY PGLASSPHHE LARKYLPKGP
GSILTFGVKG GFERAKKLIE SVKLFSFLAN VGDSKSLIVH PATVTHGQLT EAEQLLAGVK
PNQIRLSVGT EDVDDLIWDL EQALAASQR
//