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Database: UniProt
Entry: A0RXX5_CENSY
LinkDB: A0RXX5_CENSY
Original site: A0RXX5_CENSY 
ID   A0RXX5_CENSY            Unreviewed;       374 AA.
AC   A0RXX5;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Cysteine sulfinate desulfinase/cysteine desulfurase {ECO:0000313|EMBL:ABK78192.1};
DE            EC=4.4.1.- {ECO:0000313|EMBL:ABK78192.1};
GN   OrderedLocusNames=CENSYa_1572 {ECO:0000313|EMBL:ABK78192.1};
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Nitrososphaerota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004 {ECO:0000313|EMBL:ABK78192.1, ECO:0000313|Proteomes:UP000000758};
RN   [1] {ECO:0000313|EMBL:ABK78192.1, ECO:0000313|Proteomes:UP000000758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A {ECO:0000313|Proteomes:UP000000758};
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004504};
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; DP000238; ABK78192.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RXX5; -.
DR   STRING; 414004.CENSYa_1572; -.
DR   EnsemblBacteria; ABK78192; ABK78192; CENSYa_1572.
DR   KEGG; csy:CENSYa_1572; -.
DR   PATRIC; fig|414004.10.peg.1439; -.
DR   HOGENOM; CLU_003433_0_0_2; -.
DR   Proteomes; UP000000758; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000313|EMBL:ABK78192.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000758}.
FT   DOMAIN          3..349
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   374 AA;  39926 MW;  A7408F45711557CD CRC64;
     MRPEVLEAML PYLEGDYGNP SSIHRQGRTA ERAVDDAREQ AAALIGASPK EIILTSGGTE
     SNNMAVLGAR GEPGRNGFVT TSIEHDAVLE PCARLRDRGF ETSTVGPGDD GIVRAAEMAK
     AVGPGTSHAS VMTANNEVGT IQPISEIAGI CRERGAVFHT DAVQAAGKVP LDVSELGVDM
     LSFSSHKING PKGAGALYVR KGVELDPLIL GGGQERGMRS GTENVAAIAG FGRACEMARE
     RLTEDAARVR RMRDRLAERI LGEITHVEYN GSKESRLPGN AHFTFYGVSG EDLLIKLDEY
     GLAASTGSAC SVRTQKESHV LRAMGFARER INGSLRLSVG IFNTDEEIDG AVDALTRAVA
     ELRRVSPYRA KYGF
//
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