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Database: UniProt
Entry: A0A075KG90_9FIRM
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ID   A0A075KG90_9FIRM        Unreviewed;       490 AA.
AC   A0A075KG90;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU004506};
GN   ORFNames=UFO1_1747 {ECO:0000313|EMBL:AIF51298.1};
OS   Pelosinus sp. UFO1.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF51298.1, ECO:0000313|Proteomes:UP000027983};
RN   [1] {ECO:0000313|EMBL:AIF51298.1, ECO:0000313|Proteomes:UP000027983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UFO1 {ECO:0000313|EMBL:AIF51298.1};
RX   PubMed=25189589;
RA   Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L.,
RA   Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.;
RT   "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using
RT   Single-Molecule Real-Time DNA Sequencing Technology.";
RL   Genome Announc. 2:e00881-14(2014).
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC       from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC       produce L-alanine. {ECO:0000256|RuleBase:RU004506}.
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         ECO:0000256|RuleBase:RU004506};
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. Csd subfamily. {ECO:0000256|ARBA:ARBA00010447,
CC       ECO:0000256|RuleBase:RU004506}.
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DR   EMBL; CP008852; AIF51298.1; -; Genomic_DNA.
DR   RefSeq; WP_051788876.1; NZ_CP008852.1.
DR   AlphaFoldDB; A0A075KG90; -.
DR   STRING; 484770.UFO1_1747; -.
DR   KEGG; puf:UFO1_1747; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_7_2_9; -.
DR   OrthoDB; 9804366at2; -.
DR   Proteomes; UP000027983; Chromosome.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06453; SufS_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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01979; sufS; 1.
DR   PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR   PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:AIF51298.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027983};
KW   Transferase {ECO:0000256|RuleBase:RU004506}.
FT   DOMAIN          112..481
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   490 AA;  53679 MW;  FB043B96010D6FF3 CRC64;
     MTKEDGLVSA KNHWNWSPID QLAKQSCMQT AFPAQCINSH QLTQPNFLTE IRNSLASSSL
     PDSPASFDET GSYYFLTPSS APLTLTSQEL DVEAIRRDFP ALHQQVNGRP LIWLDNAATT
     QKPQSVITAV AQFYSQDNSN VHRGAHTLAK RATDAYEGAR KKVMNLIGAS SPDEIVFVRG
     ATEAINLVAQ SYGRRIVGPG DEIIVSILDH HANIVPWQLL CEEKDAILRV IPVNEHAELI
     IEEYEKLLSP KTRLIAIPHV SNSLGTVIPI KTIIDMAHSR NIPVLVDGAQ GLPHFQTNVQ
     DLGVDFYAFS GHKLFGPTGI GVLYGKKDLL EAMPPWQGGG NMIKDVTFEN TTFNSLPNKF
     EAGTGHISGA VGLGAAIDYL TNLGFSKIER YEKNLLSYAT EALGNIPKLH LVGTSTHKAG
     ILSFVVPGVP SERIAEFLDK QGIALRVGHH CAQPSLRSFG LESTIRPSIA FYNTFSEIEK
     LVWAIRKSIQ
//
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