ID A0A037ZKK8_9RHOB Unreviewed; 391 AA.
AC A0A037ZKK8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=cysteine-S-conjugate beta-lyase {ECO:0000256|ARBA:ARBA00012224};
DE EC=4.4.1.13 {ECO:0000256|ARBA:ARBA00012224};
GN ORFNames=ACMU_00200 {ECO:0000313|EMBL:KAJ56946.1};
OS Actibacterium mucosum KCTC 23349.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Actibacterium.
OX NCBI_TaxID=1454373 {ECO:0000313|EMBL:KAJ56946.1, ECO:0000313|Proteomes:UP000026249};
RN [1] {ECO:0000313|EMBL:KAJ56946.1, ECO:0000313|Proteomes:UP000026249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 23349 {ECO:0000313|EMBL:KAJ56946.1,
RC ECO:0000313|Proteomes:UP000026249};
RA Arahal D.R., Shao Z., Lai Q., Pujalte M.J.;
RT "Draft Genome Sequence of Actibacterium mucosum KCTC 23349, a Marine
RT Alphaproteobacterium with Complex Ionic Requirements Isolated from
RT Mediterranean Seawater at Malvarrosa Beach, Valencia, Spain.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
CC {ECO:0000256|ARBA:ARBA00037974}.
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:KAJ56946.1}.
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DR EMBL; JFKE01000001; KAJ56946.1; -; Genomic_DNA.
DR RefSeq; WP_035255065.1; NZ_JFKE01000001.1.
DR AlphaFoldDB; A0A037ZKK8; -.
DR STRING; 1454373.ACMU_00200; -.
DR OrthoDB; 3224382at2; -.
DR Proteomes; UP000026249; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR027619; C-S_lyase_PatB-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04350; C_S_lyase_PatB; 1.
DR PANTHER; PTHR43525; PROTEIN MALY; 1.
DR PANTHER; PTHR43525:SF1; PROTEIN MALY; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KAJ56946.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000026249};
KW Transferase {ECO:0000313|EMBL:KAJ56946.1}.
FT DOMAIN 56..383
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 391 AA; 43425 MW; 9CDAAB0A31D6E6BA CRC64;
MNFDEIIDRR GTNSSKWDGM EKSIGVSAED GIAMWVADMD FRAPDFLQAA TQQLLDQANY
GYFTGVDAYF DAAAWWMQTR HGWAMDPSWL FVTFGLGNGI GLALQSLTEP GDEIVTFTPV
YHEFARRITK GGRVVRELPL QTDENGLYRM DFDHYDTLMS GREKMVLFCS PHNPAGRVWT
QAEIDAFADF VVKHDLLVVS DEIHHDLTFP GQKHLPLHVA APQLEDRLIM MTSASKTFNI
AGARTGLVAI PNPSLRAKYG ALYTALDMSP NLHGVRLSQA AYSTEGAEWV DALNQYLEEN
ASHFINRIDA IPGLKAMPMQ STYLAWVDFA GTGMERAEFA SRVADTARIG TTPGHSLGSG
GETFLRFNLG TPRARIDEAL TRLQSAFSDL Q
//
