ID I2F3E0_9BACT Unreviewed; 374 AA.
AC I2F3E0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Cysteine desulfurase family protein {ECO:0000313|EMBL:AFK06443.1};
GN ORFNames=Theba_0726 {ECO:0000313|EMBL:AFK06443.1};
OS Mesotoga prima MesG1.Ag.4.2.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX NCBI_TaxID=660470 {ECO:0000313|EMBL:AFK06443.1, ECO:0000313|Proteomes:UP000002881};
RN [1] {ECO:0000313|EMBL:AFK06443.1, ECO:0000313|Proteomes:UP000002881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mesG1.Ag.4.2 {ECO:0000313|Proteomes:UP000002881};
RX PubMed=22798451;
RA Zhaxybayeva O., Swithers K.S., Foght J., Green A.G., Bruce D., Detter C.,
RA Han S., Teshima H., Han J., Woyke T., Pitluck S., Nolan M., Ivanova N.,
RA Pati A., Land M.L., Dlutek M., Doolittle W.F., Noll K.M., Nesbo C.L.;
RT "Genome Sequence of the Mesophilic Thermotogales Bacterium Mesotoga prima
RT MesG1.Ag.4.2 Reveals the Largest Thermotogales Genome To Date.";
RL Genome Biol. Evol. 4:700-708(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001357};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; CP003532; AFK06443.1; -; Genomic_DNA.
DR RefSeq; WP_014730501.1; NC_017934.1.
DR AlphaFoldDB; I2F3E0; -.
DR STRING; 660470.Theba_0726; -.
DR KEGG; mpg:Theba_0726; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_2_0; -.
DR Proteomes; UP000002881; Chromosome.
DR Gene3D; 1.10.260.50; -; 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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002881}.
FT DOMAIN 3..359
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 374 AA; 41506 MW; A54ADA1285F5E44C CRC64;
MRYFDNNATT KMESDLAERF AKLCVEEYAN PNSMHSFGLR EARYLEEARR KIARSLSSDP
REIYFTSCAT ESINWILRSS VLFKGRRKRI VTTSIEHKAV LNTLKDLKAS SDIDYRTVGP
ERNGIVKVAK LLDEVDEETF LVSLMAVNNV TGAIQPYEEI GEELRRRNVL FHLDAVQTIG
KIPIDFVSCF CDYASFSAHK FHGPKGVGVT YVRQGTPIRP LITGGGQERG MRSGTQNVPG
AVIAATALQR AVECTQESSS RLREYQHRIK ETVEELDGVV NTPENSISNT VNASFAGIRS
EVLVNALSEE GVFVGTSSAC SSRGDGGQYV LDSMGLDFSL ASSSIRISMS RFTTEEDVAF
LIEKLKKTVP LLKF
//