ID F2NPA4_MARHT Unreviewed; 418 AA.
AC F2NPA4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Cysteine synthase {ECO:0000313|EMBL:AEB11905.1};
DE EC=2.5.1.47 {ECO:0000313|EMBL:AEB11905.1};
GN OrderedLocusNames=Marky_1165 {ECO:0000313|EMBL:AEB11905.1};
OS Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Marinithermus.
OX NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB11905.1, ECO:0000313|Proteomes:UP000007030};
RN [1] {ECO:0000313|EMBL:AEB11905.1, ECO:0000313|Proteomes:UP000007030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX PubMed=22675595; DOI=10.4056/sigs.2435521;
RA Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Pan C., Brambilla E.M., Rohde M., Tindall B.J., Sikorski J.,
RA Goker M., Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT chimney.";
RL Stand. Genomic Sci. 6:21-30(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; CP002630; AEB11905.1; -; Genomic_DNA.
DR RefSeq; WP_013703952.1; NC_015387.1.
DR AlphaFoldDB; F2NPA4; -.
DR STRING; 869210.Marky_1165; -.
DR KEGG; mhd:Marky_1165; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_0; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000007030; 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:UP000007030};
KW Transferase {ECO:0000313|EMBL:AEB11905.1}.
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 418 AA; 44950 MW; D975F9D138DE1E20 CRC64;
MGKDLEYATL AVQTGLPENP YDALGLPIYP VAAYQFGSLE EGADRFANAT GYTYSRLQNP
TVAALEERLA ALEGALGAVA LSAGNAATFA ALLALVKTGD AIVASPGLFG GTVGLLNNVF
SLMGVEVRYA APEADAVRAV LDERVRVIFT ESLANPALTL PDLEGLAALA EERGVALVVD
NTFGSLGYLL RPLEHGAHVV VHSLTKWASG HGSVLGGAVL SRETELWQRY PQFVNPTPQG
FVPLERFGAR CYLERVRNLG LQLGGMVLSP FNAYLIHQGL ETLALRAERA SRTAHRLAEW
LREHPKVAWV RYPGLEDHPD HARARKYLKH FGTILTFGVK GGMEAASRLL RAIRLLRQAP
NVGDARTLIL HPWTTTHGRL PEAARRAAGV APEMLRISVG LEDPADLEAA LGEALEAV
//
