ID A0A0T7BYF4_9CYAN Unreviewed; 402 AA.
AC A0A0T7BYF4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU364075};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239, ECO:0000256|RuleBase:RU364075};
DE AltName: Full=Nitrogenase metalloclusters biosynthesis protein NifS {ECO:0000256|RuleBase:RU364075};
GN ORFNames=IJ00_25000 {ECO:0000313|EMBL:AKG24142.1};
OS Calothrix sp. 336/3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1337936 {ECO:0000313|EMBL:AKG24142.1, ECO:0000313|Proteomes:UP000065745};
RN [1] {ECO:0000313|EMBL:AKG24142.1, ECO:0000313|Proteomes:UP000065745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=336/3 {ECO:0000313|EMBL:AKG24142.1,
RC ECO:0000313|Proteomes:UP000065745};
RX PubMed=25614574;
RA Isojarvi J., Shunmugam S., Sivonen K., Allahverdiyeva Y., Aro E.M.,
RA Battchikova N.;
RT "Draft genome sequence of calothrix strain 336/3, a novel h2-producing
RT cyanobacterium isolated from a finnish lake.";
RL Genome Announc. 3:0-0(2015).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine
CC to produce alanine. Seems to participate in the biosynthesis of the
CC nitrogenase metalloclusters by providing the inorganic sulfur required
CC for the Fe-S core formation. {ECO:0000256|ARBA:ARBA00003120}.
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|RuleBase:RU364075};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490, ECO:0000256|RuleBase:RU364075}.
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DR EMBL; CP011382; AKG24142.1; -; Genomic_DNA.
DR RefSeq; WP_035158000.1; NZ_CP011382.1.
DR AlphaFoldDB; A0A0T7BYF4; -.
DR STRING; 1337936.IJ00_25000; -.
DR KEGG; calh:IJ00_25000; -.
DR eggNOG; COG1104; Bacteria.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000065745; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR017772; Cys_deSase_NifS_bac/arc.
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; TIGR03402; FeS_nifS; 1.
DR PANTHER; PTHR11601:SF63; CYSTEINE DESULFURASE; 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, ECO:0000256|RuleBase:RU364075};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364075};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364075};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU364075};
KW Reference proteome {ECO:0000313|Proteomes:UP000065745};
KW Transferase {ECO:0000256|RuleBase:RU364075}.
FT DOMAIN 6..367
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 402 AA; 43877 MW; BEEC706F7E431B3D CRC64;
MQRNCIYLDN NATTKVDPAV VEAMMPYITD YYGNPSSMHT FGGQVAKAVK IAREQVAALL
GADETEIVFT SGGTEGDNAA IRAALLAQPE KRHIITTQVE HPAVLTLCKQ LETQGYSVTY
LSVNQHGQLD LDELDAALTG NTALVSIMYA NNETGTVFPI EEIGARVKAK GAIFHVDAVQ
AVGKLPLNMK NSTIDMLVMS GHKIHAPKGI GALYIRRGVR FRPLIIGGGQ QRGRRAGTEN
VPGLVALGKA AELELLHMEE ATAREIKQRD RLEKTILSLI SDCEVNGDIT QRLPNTTNIG
FKYIEGEAIL LHLNQHQICA SSGSACSSGS LEPSHVLRAM GLPYTTLHGS IRFSLCRYTT
EAEIDKVIEV LPGIIQHLRD LSPFKNDQAA WLQQHEQVLT HR
//
