ID I4ER26_9ACTN Unreviewed; 430 AA.
AC I4ER26;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=O-acetylhomoserine/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:CCH85839.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:CCH85839.1};
GN Name=metC {ECO:0000313|EMBL:CCH85839.1};
GN OrderedLocusNames=MODMU_0381 {ECO:0000313|EMBL:CCH85839.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH85839.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH85839.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH85839.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(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}.
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DR EMBL; FO203431; CCH85839.1; -; Genomic_DNA.
DR RefSeq; WP_014738453.1; NC_017955.1.
DR AlphaFoldDB; I4ER26; -.
DR STRING; 477641.MODMU_0381; -.
DR KEGG; mmar:MODMU_0381; -.
DR PATRIC; fig|477641.3.peg.358; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_11; -.
DR OMA; YGGMITF; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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:UP000006461};
KW Transferase {ECO:0000313|EMBL:CCH85839.1}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 430 AA; 45602 MW; 515F6B5BB5B07E20 CRC64;
MADRTWGFRT RALHAGGAPD PTTGARAVPI YQTTSFVFDS ADDAANLFAL QKYGNVYSRI
ANPTVAALEE RIASLEGGLG AVATSSGQAA EFLTFAALAG AGDHIVAASS LYGGTITQLD
VTLRRFGVET TFVRGNDPAD YAAAITDRTK LVFAEVVANP GSDVADIAGL AEVAHAAGVP
LVVDATTATP WLCRPIEHGA DIVIHSATKF LGGHGTTLGG LVVDAGTFDW GNGRFPGMTE
PSDSYGGIRW WDNFGEYGFL TKLRSEQLRD VGATLAPHSA FLLLMGIETL PQRMREHVAN
AQRVAEWLDA DERVAWVRYS GLPGHRDHAL AQRYLPEGPG AVFSFGVVGG RDAGRRFIEN
VELCSHLANI GDARTLVIHP GSTTHGQLSV EQLETGGVSP DLIRISVGLE DVEDVLWDLD
QALAAAVKDV
//
