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Database: UniProt
Entry: A0A061NP36_9BACL
LinkDB: A0A061NP36_9BACL
Original site: A0A061NP36_9BACL 
ID   A0A061NP36_9BACL        Unreviewed;       425 AA.
AC   A0A061NP36;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:GAK06413.1};
GN   ORFNames=JCM19038_107 {ECO:0000313|EMBL:GAK06413.1};
OS   Geomicrobium sp. JCM 19038.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX   NCBI_TaxID=1460635 {ECO:0000313|EMBL:GAK06413.1, ECO:0000313|Proteomes:UP000027014};
RN   [1] {ECO:0000313|EMBL:GAK06413.1, ECO:0000313|Proteomes:UP000027014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19038 {ECO:0000313|EMBL:GAK06413.1,
RC   ECO:0000313|Proteomes:UP000027014};
RA   Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA   Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA   Hongoh Y., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT   JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL   Genome Announc. 2:e00622-14(2014).
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:GAK06413.1}.
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DR   EMBL; BAXA01000001; GAK06413.1; -; Genomic_DNA.
DR   RefSeq; WP_042413429.1; NZ_BAXA01000001.1.
DR   AlphaFoldDB; A0A061NP36; -.
DR   eggNOG; COG2873; Bacteria.
DR   Proteomes; UP000027014; 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   Reference proteome {ECO:0000313|Proteomes:UP000027014}.
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   425 AA;  46046 MW;  EFD1B55CBE822F11 CRC64;
     MSETWKLETK AIHSGQEIDQ STGARAVPIY QTTSYGFDNA DHAANLFSLQ ENGNIYTRIM
     NPTQAVFEDR IADLEGGVAA LATASGSSAI HLAILNICRS GDEVVASSSL YGGTYNLFKH
     TLPEMGINVR FVDIDDPNAY KAAITDKTKA VYGELIGNPD GKILDIEAVA NVAHEAGLPL
     IVDATLATPY LCRPIEHGAD IVVHSATKFI GGHGTSIAGV IVDSGRFDWT HGNFPMFTEP
     DPSYHGVVFS EAVGELAYII RARVRLLRDL GPAISPQNAF LMLQGLETLH LRMERHVENA
     KKVTEYLEKH SSVDWVSYAG SAKHESYSLA EKYFSYGPGA VLTFGIKGGH EAGKAFINQV
     KLHSHVANVG DAKSLIIHPA STTHQQLTED EQKQAGVSPE LIRLSVGIEH ADDIIADLEQ
     AFREV
//
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