ID C0N9B2_9GAMM Unreviewed; 424 AA.
AC C0N9B2;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase subfamily {ECO:0000313|EMBL:EEF78547.1};
GN ORFNames=MDMS009_2720 {ECO:0000313|EMBL:EEF78547.1};
OS Methylophaga thiooxydans DMS010.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=637616 {ECO:0000313|EMBL:EEF78547.1, ECO:0000313|Proteomes:UP000004679};
RN [1] {ECO:0000313|EMBL:EEF78547.1, ECO:0000313|Proteomes:UP000004679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMS010 {ECO:0000313|EMBL:EEF78547.1,
RC ECO:0000313|Proteomes:UP000004679};
RX PubMed=21478352; DOI=10.1128/JB.00388-11;
RA Boden R., Ferriera S., Johnson J., Kelly D.P., Murrell J.C., Schafer H.;
RT "Draft genome sequence of the chemolithoheterotrophic, halophilic
RT methylotroph Methylophaga thiooxydans DMS010.";
RL J. Bacteriol. 193:3154-3155(2011).
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}.
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DR EMBL; GG657906; EEF78547.1; -; Genomic_DNA.
DR RefSeq; WP_008292085.1; NZ_GG657906.1.
DR AlphaFoldDB; C0N9B2; -.
DR HOGENOM; CLU_018986_4_2_6; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000004679; 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:UP000004679};
KW Transferase {ECO:0000313|EMBL:EEF78547.1}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 424 AA; 46053 MW; 4DBF59354BB82A21 CRC64;
MKIETLCLHE GYETDPVTKS CAVPIYQTVA YEFDNAQHGA DLFNLDVPGN IYSRIMNPTW
DVLEKRVAAL EGGLAALAVS AGSAAIHYAI LTIAEAGDNI VTTPQLYGGT YTLFAHMLPK
LGIEVRFAAT DQPEAMASLI DDNTKAVFCE TIGNPAGNII DIEAVAQLAH AQGVPLIVDN
TVATPALLRP IDYGADIVVH SLTKYMGGHG TTLGGIIVDS GKFPWTQHKA KFPMLNEPEA
AYHGVVYTEQ FGEAAFIARA RTVPLRNTGS ALSPMNAFML LQGIETLPLR MERHCENAAA
VAEFLSQHDK VEWVNYAGLE TDKYHRLAQK YFDGKPSSLL TFGIKGGFEA GVKFYDALNM
IKRLVNIGDT KTLACHPAST THRQLEPHEL KTAGVTPEML RLCVGIEHID DILADISQAF
EAVK
//