ID D3NVR5_AZOS1 Unreviewed; 431 AA.
AC D3NVR5;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:BAI72494.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:BAI72494.1};
GN Name=metY {ECO:0000313|EMBL:BAI72494.1};
GN OrderedLocusNames=AZL_018560 {ECO:0000313|EMBL:BAI72494.1};
OS Azospirillum sp. (strain B510).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI72494.1, ECO:0000313|Proteomes:UP000002040};
RN [1] {ECO:0000313|EMBL:BAI72494.1, ECO:0000313|Proteomes:UP000002040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B510 {ECO:0000313|EMBL:BAI72494.1,
RC ECO:0000313|Proteomes:UP000002040};
RX PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA Nakayama S., Yamada M., Tabata S., Sato S.;
RT "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT sp. B510.";
RL DNA Res. 17:37-50(2010).
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; AP010946; BAI72494.1; -; Genomic_DNA.
DR RefSeq; WP_012974469.1; NC_013854.1.
DR AlphaFoldDB; D3NVR5; -.
DR STRING; 137722.AZL_018560; -.
DR KEGG; azl:AZL_018560; -.
DR HOGENOM; CLU_018986_4_0_5; -.
DR OrthoDB; 9790858at2; -.
DR Proteomes; UP000002040; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:BAI72494.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002040};
KW Transferase {ECO:0000313|EMBL:BAI72494.1}.
FT MOD_RES 211
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 431 AA; 45586 MW; DB0D75103456D50C CRC64;
MTEQKSFGFE TRAIHAGAAP DPATGARQTP IYQTTSFVFE DVDDAASLFN LQKVGFIYSR
LTNPTVAVLE ERLANLEGGA GATATASGHA AQLLALFPLM APGDHIVASK KLYGGSLNQL
GISFPRAFGW QPSFVDTDDV ETVKVALTEK TKAIFVESLA NPGGVVTDIE AIAKIADEAG
IPLIVDNTLA TPYLINPIDW GATLVVHSTT KFLSGNGTSV GGVVVDSGKF DWSKSGKFPA
LSEPDPGYHG LRFHETFGHL AFTIHGHAVG LRDLGPSQAP MNAFLTLNGI ETLPLRMQRH
ADSALKVARF LESHPAVSWV SYAGLESSKY NALARKYLPR GAGAVLTFGV KGGFEAGVKM
VESVELFSHL ANIGDARSLI IHPSSTTHRQ LSAEAQASAG AGPEVIRLSI GLETPEDIIA
DLDQALSKTL A
//
