ID F2NNU9_MARHT Unreviewed; 375 AA.
AC F2NNU9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Cys/Met metabolism pyridoxal-phosphate-dependent protein {ECO:0000313|EMBL:AEB11323.1};
GN OrderedLocusNames=Marky_0572 {ECO:0000313|EMBL:AEB11323.1};
OS Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Marinithermus.
OX NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB11323.1, ECO:0000313|Proteomes:UP000007030};
RN [1] {ECO:0000313|EMBL:AEB11323.1, 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; AEB11323.1; -; Genomic_DNA.
DR RefSeq; WP_013703375.1; NC_015387.1.
DR AlphaFoldDB; F2NNU9; -.
DR STRING; 869210.Marky_0572; -.
DR KEGG; mhd:Marky_0572; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_0; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000007030; Chromosome.
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:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 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:UP000007030}.
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 375 AA; 40047 MW; 82251B45FA3E62FC CRC64;
MRLETLAIHA GRAVDPATGA VRPPIHLSTT FERDPDGGYA RGYVYARYGN PNRAALEEAL
AALEGGAAAL AFASGSAATM SVFQALEPGD HVVAPLDAYH GTVGLLREHF TRWGLEVTFA
DLTDPEQLEA ALRPNTRLVW VETPSNPLLR ITDIRRVVEA AHAVGARVVC DNTWATPVLQ
RPLALGCDLV VHATTKYLNG HGDVTGGVVV AREVDAWFER LRAIQVQGGA VPSPFDAWLV
LRGLATLPYR VRAHTEHAAR VAAFLQAHPA VEAVHYPGLA DHPGHAVAAR QMEGFGGMLA
FQVRGGREAA LAVAARVRLI TRATSLGGVE SLIEHRASIE GPGTRTPENL LRLSVGLEHP
EDLIADLEQA LEAAV
//
