ID B6BMD5_SULGG Unreviewed; 411 AA.
AC B6BMD5; H1FWP6;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Putative O-acetylhomoserine/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:EHP29287.1};
GN ORFNames=SMGD1_0760 {ECO:0000313|EMBL:EHP29287.1};
OS Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP29287.1, ECO:0000313|Proteomes:UP000006431};
RN [1] {ECO:0000313|EMBL:EHP29287.1, ECO:0000313|Proteomes:UP000006431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD1 {ECO:0000313|EMBL:EHP29287.1,
RC ECO:0000313|Proteomes:UP000006431};
RX PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA Labrenz M., Jurgens K.;
RT "Genome and physiology of a model Epsilonproteobacterium responsible for
RT sulfide detoxification in marine oxygen depletion zones.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:506-510(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:EHP29287.1}.
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DR EMBL; AFRZ01000001; EHP29287.1; -; Genomic_DNA.
DR RefSeq; WP_008338814.1; NZ_DS995290.1.
DR AlphaFoldDB; B6BMD5; -.
DR STRING; 929558.SMGD1_0760; -.
DR PATRIC; fig|929558.5.peg.759; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_2_0_7; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000006431; 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 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 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006431}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 411 AA; 44514 MW; 4A3ECB5BE92DD92C CRC64;
MNNFEEYCTK FVQSVGNKEG AVSPAVINSA SFAYDTPEIA EGIFDGSVKK PLYARMGNPT
TAKLESIMAD MDGGVAAVAT SSGMGATTLA CMSLLASGDE IISIGGLFGG TYALFSETLT
RFGIKTRFFD VDDFKEIEEA INDNTKIIFL ESVGNPNMKL PDIKRIAKIA NDAGVILIID
NTITPLSISP LKLGADISVY STTKIISGNA SALGGCAVFR AVNDGEDKLK SPRYEFLAKF
IKGAGKMALF ANAKKRALRD FGMSANANAS YQTMLGLETL PLRLSRITHS VEVVASTLSE
NGLNINHPCL KTHPHHNRYI NDFKNGCGTL FTIDMGSKQR AFEFLNNTKL ATLTANIGDN
RTLALHMAST IYRDFDEETR KFLGITDGLI RISIGLENPQ DIIDDFIQAH K
//
