ID A0A0F8AVN6_9EURY Unreviewed; 425 AA.
AC A0A0F8AVN6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=FK85_24680 {ECO:0000313|EMBL:KKF39916.1};
OS Halorubrum saccharovorum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=2248 {ECO:0000313|EMBL:KKF39916.1, ECO:0000313|Proteomes:UP000053331};
RN [1] {ECO:0000313|EMBL:KKF39916.1, ECO:0000313|Proteomes:UP000053331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|EMBL:KKF39916.1,
RC ECO:0000313|Proteomes:UP000053331};
RA Rozanov A.S., Kotenko A.V., Bryanskaya A.V., Malup T.K., Peltek S.E.;
RT "Full genome sequence of Halorubrum H3 strain isolated from Burlinskoye
RT Salt Lake (Altai Krai, Russia).";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKF39916.1}.
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DR EMBL; JNFH02000009; KKF39916.1; -; Genomic_DNA.
DR RefSeq; WP_050023666.1; NZ_JNFH02000009.1.
DR AlphaFoldDB; A0A0F8AVN6; -.
DR OrthoDB; 5817at2157; -.
DR Proteomes; UP000053331; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-UniRule.
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; IPR016454; Cysteine_dSase.
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:SF8; CYSTEINE DESULFURASE-RELATED; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004506};
KW Reference proteome {ECO:0000313|Proteomes:UP000053331};
KW Transferase {ECO:0000256|RuleBase:RU004506}.
FT DOMAIN 43..413
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 425 AA; 46114 MW; 24A916B34E0A8591 CRC64;
MGVQEQYPFD VEAVRADFPI LDRKVGGDPE TPGEGPGDDT PLVYLDSAAT SHTPDAVVDT
IADYYRGYNA NVHRGIHQLS QEASVAYEQA HDTVADFIGA SGREEVVFTK NTTEAMNLVA
YAWGLEELGP GDNVVLSQME HHSSLVTWQQ IGKRTGADVR FIEVTDEGRL DMEHAAECID
DDTQMVSVVH VSNTLGTVNP IPEIAAMAHD HDAYVFADGA QSVPTRPVDV KDLGVDFLAF
SGHKMCGPTG IGALYGREEI LDEMGPYLYG GDMIRRVSFE DSTWEDLPWK FEAGTPSIAQ
GIAFAAAIEY LEEIGMENVQ AHEDLLAEYA YDELTDLGGV EIYGPPGHDR GGLVAFNVEG
VHAHDLSSIL NDYGVAIRAG DHCTQPLHDE MGVAASARAS FYLYNTVEEI DALVEAVGEA
RDLFA
//
