ID A0A1F8JSS3_9BACT Unreviewed; 374 AA.
AC A0A1F8JSS3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=A3E80_03730 {ECO:0000313|EMBL:OGN65085.1};
OS Chlamydiae bacterium RIFCSPHIGHO2_12_FULL_49_9.
OC Bacteria; Chlamydiota.
OX NCBI_TaxID=1797605 {ECO:0000313|EMBL:OGN65085.1, ECO:0000313|Proteomes:UP000176727};
RN [1] {ECO:0000313|EMBL:OGN65085.1, ECO:0000313|Proteomes:UP000176727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:OGN65085.1}.
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DR EMBL; MGLY01000023; OGN65085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8JSS3; -.
DR Proteomes; UP000176727; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; 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; 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: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.
PE 4: Predicted;
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 6..357
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 374 AA; 40426 MW; 4A62E472BAE3FFAF CRC64;
MYSQRIYLDN NATTELDPSV LEAMLKELKG PPANPSSVHS FGIDARKLLT SARKTVADFF
HAKPEEVTFT SGGTESLNLL LRGLKPKSHL LTTRLEHSAI HETLKSLDLD VTYLPVGTKG
APTPAQIESA IRPDTKGILL SYSNGETGVK IDLTAIAQIA REKNVPLFID AVSAIGKERL
DLPKGVSALA LSAHKFHGPK GVGALLLRSP HKPSPLLTGG AQELNLRAGT ENLAGIIGLA
KAIELLQEKQ PSITEHLLFL RNRFEKGLFD SLPDIAINGE GPRIANASNI AFFGVDGESL
LLHLDLNHIA ASHGSACASG SLEPSRILLE MGIDRKRARS SIRFSFSRMN RVEEIDRAVQ
IISTLVKKLR KISA
//
