ID A6TUF8_ALKMQ Unreviewed; 380 AA.
AC A6TUF8;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ABR49826.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:ABR49826.1};
GN OrderedLocusNames=Amet_3706 {ECO:0000313|EMBL:ABR49826.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR49826.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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|RuleBase:RU362118}.
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DR EMBL; CP000724; ABR49826.1; -; Genomic_DNA.
DR RefSeq; WP_012064786.1; NC_009633.1.
DR AlphaFoldDB; A6TUF8; -.
DR STRING; 293826.Amet_3706; -.
DR KEGG; amt:Amet_3706; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_1_9; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000001572; Chromosome.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF15; CYSTATHIONINE GAMMA-LYASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 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:UP000001572};
KW Transferase {ECO:0000313|EMBL:ABR49826.1}.
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 380 AA; 41758 MW; 300ED53706DC86ED CRC64;
MNFGTKLIHN TNDKDKITGA LSIPIYQVST YHQEDIEAEQ EYQYSRSENP TRRAIEETIA
ELENGDRGFA FSSGMAATSS VLSIFSAGDH IIACQDVYGG TYRALNRIFN RYGIEVSLVD
TTDLGEIEAN IKENTRAIFL ETPSNPTLKI TNLKGAVGIA KAHHLLVIVD NTFMTPYLQR
PLDLGADIVI HSATKFIGGH SDVVAGLVAV KGKALSERLY MIQNGFGAVL GPQDSWLLLR
GLKTLKVRMD YQQKNAEELA QWLSNHEKIQ KVYYPGLLGH QNREIHDTQA NGAGAVMSFK
TVEIETAQKF MKMVKLAAVA VSLGGVETIA SYPVKMSHAA MPKAQRESLG ITENLIRLSV
GLEDIKDLIE DFDKALAGAE
//
