ID F2ATX1_RHOBT Unreviewed; 439 AA.
AC F2ATX1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=O-acetylhomoserine/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:EGF26955.1};
DE EC=2.5.1.- {ECO:0000313|EMBL:EGF26955.1};
GN ORFNames=RBWH47_03994 {ECO:0000313|EMBL:EGF26955.1};
OS Rhodopirellula baltica WH47.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=991778 {ECO:0000313|EMBL:EGF26955.1, ECO:0000313|Proteomes:UP000006222};
RN [1] {ECO:0000313|EMBL:EGF26955.1, ECO:0000313|Proteomes:UP000006222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH47 {ECO:0000313|EMBL:EGF26955.1,
RC ECO:0000313|Proteomes:UP000006222};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
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}.
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:EGF26955.1}.
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DR EMBL; AFAR01000168; EGF26955.1; -; Genomic_DNA.
DR RefSeq; WP_007327082.1; NZ_AFAR01000168.1.
DR AlphaFoldDB; F2ATX1; -.
DR PATRIC; fig|991778.3.peg.3365; -.
DR Proteomes; UP000006222; Unassembled WGS sequence.
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 Transferase {ECO:0000313|EMBL:EGF26955.1}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 215
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 439 AA; 47670 MW; D84355300C619690 CRC64;
MSADPTQNHR LATRALHAGQ VADPTTKSRA VPIYATTSYQ FDSTEHAAAL FGLAEFGNIY
SRLMNPTVDV LEKRIAALDG GVTGLCFASG QAAITAAVLA IAHSGQNIVS STSLYGGTWT
LFTQTLKNLG IEVRFFDPDH PEQIHGLVDE NTRLVYMESI GNPRNDVPDF KAIADAAHSA
PHGAIPVLCD NTVMTPYLLR PIDHGIDIVI YSTTKFLGGH GTHIGGCIVD SGNFKWADQP
EKWPEFCGPS PSYHGAVFEE HLRGMGNIAY NVHIRTHWLR DTGAAMSPFA AFLFLQGIET
LHLRMPRHCE NAMKVAEFLE AHDAVEWVNY PGLKTHSHNK LAEQYLTNGK GAILGFGIKG
GMEAGKKFIN ACQLCSHLAN IGDAKTLVIH PASTTHQQLA EDEQRRAGVS PEYIRVSVGI
EDIDDILDDL KQALAVATA
//
