ID A6TJD2_ALKMQ Unreviewed; 411 AA.
AC A6TJD2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Cysteine synthase {ECO:0000313|EMBL:ABR46300.1};
DE EC=2.5.1.47 {ECO:0000313|EMBL:ABR46300.1};
GN OrderedLocusNames=Amet_0057 {ECO:0000313|EMBL:ABR46300.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR46300.1, 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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR EMBL; CP000724; ABR46300.1; -; Genomic_DNA.
DR RefSeq; WP_011971209.1; NC_009633.1.
DR AlphaFoldDB; A6TJD2; -.
DR STRING; 293826.Amet_0057; -.
DR KEGG; amt:Amet_0057; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_9; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000001572; Chromosome.
DR GO; GO:0004124; F:cysteine synthase 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 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001572};
KW Transferase {ECO:0000313|EMBL:ABR46300.1}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 411 AA; 45313 MW; 8DC51AD7D2E6C043 CRC64;
MGLNTKLIHG NGVSKEKKVG ATNVPIYFSN AYAYNKAKDL ENIFSGRDIG HVYTRISNPS
IEALEKRMVA VEGGVSAIAT ASGMSAIYLA VMNILTPGDE IIASSGVFGG TYNFFKNLKQ
LNIEVKFVDE LNEESLTEHI TPKTKIVFAE TIGNPKLDVL DIEVVSTICK IKGVVFMVDS
TVTTPYLIRP LEYGADVVIH SVSKYVNGSA NSIGGMIIDG GSTKFNSERY ENFKHYTKRY
RQFAFSAKLR NELGKDLGAV MSPMNSFLNL TGIETLSLRM KRHCHNAYQL AKYLQENPKV
LHTNYPGLET SEYYPLTQKY YAKEAGGILT LRVGSKEKAF QLIDSLKLIS NVTNIGDTKT
LALHPASTIC NGNTPEEKEQ MGVYEDLIRV SVGLEDMEDI IEDLENALGG L
//
