ID   CYD_MYCPA               Reviewed;         685 AA.
AC   Q9KII6;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Probable cysteine desulfurase;
DE            EC=2.8.1.7;
GN   Name=cyd {ECO:0000250|UniProtKB:Q8KUU5}; OrderedLocusNames=MAP_2120c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19698 / CIP 103963 / DSM 44133 / TMC 807;
RX   PubMed=11549181; DOI=10.1099/0022-1317-50-9-795;
RA   Bannantine J.P., Stabel J.R.;
RT   "Identification of two Mycobacterium avium subspecies paratuberculosis gene
RT   products differentially recognised by sera from rabbits immunised with live
RT   mycobacteria but not heat-killed mycobacteria.";
RL   J. Med. Microbiol. 50:795-804(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TYPE 2A ENCAPSULIN,
RP   SUBUNIT, SUBCELLULAR LOCATION, AND ANTIGENICITY.
RC   STRAIN=509;
RX   PubMed=25500374; DOI=10.1016/j.vetmic.2014.11.009;
RA   Leite F.L., Reinhardt T.A., Bannantine J.P., Stabel J.R.;
RT   "Envelope protein complexes of Mycobacterium avium subsp. paratuberculosis
RT   and their antigenicity.";
RL   Vet. Microbiol. 175:275-285(2015).
CC   -!- FUNCTION: Cargo protein of a type 2A encapsulin nanocompartment
CC       involved in sulfur metabolism. Cysteine desulfurases mobilize the
CC       sulfur from L-cysteine to yield L-alanine, an essential step in sulfur
CC       metabolism for biosynthesis of a variety of sulfur-containing
CC       biomolecules. {ECO:0000250|UniProtKB:Q8KUU5}.
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:0000250|UniProtKB:Q8KUU5};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P77444};
CC   -!- SUBUNIT: Isolated from bacteria in a complex with encapsulin 2A (AC
CC       I3NID5), strongly suggesting it is found in a type 2A encapsulin
CC       nanocompartment (PubMed:25500374). There are 1-2 copies of this protein
CC       in each encapsulin shell (By similarity).
CC       {ECO:0000250|UniProtKB:Q8KUU5, ECO:0000269|PubMed:25500374}.
CC   -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment
CC       {ECO:0000250|UniProtKB:Q8KUU5, ECO:0000305}. Cell membrane
CC       {ECO:0000305|PubMed:25500374}.
CC   -!- MISCELLANEOUS: Cattle naturally infected with M.paratuberculosis have
CC       antisera that recognize this protein. {ECO:0000269|PubMed:25500374}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS04437.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF232751; AAF82074.1; -; Genomic_DNA.
DR   EMBL; AE016958; AAS04437.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q9KII6; -.
DR   SMR; Q9KII6; -.
DR   STRING; 262316.MAP_2120c; -.
DR   EnsemblBacteria; AAS04437; AAS04437; MAP_2120c.
DR   KEGG; mpa:MAP_2120c; -.
DR   eggNOG; COG0520; Bacteria.
DR   HOGENOM; CLU_003433_7_0_11; -.
DR   OMA; AETPPWQ; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   CDD; cd06453; SufS_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
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   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01979; sufS; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Encapsulin nanocompartment; Membrane; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..685
FT                   /note="Probable cysteine desulfurase"
FT                   /id="PRO_0000150303"
FT   REGION          1..282
FT                   /note="Cargo-loading domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KUU5"
FT   REGION          48..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..121
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..178
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        640
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P77444"
FT   MOD_RES         502
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P77444"
SQ   SEQUENCE   685 AA;  71595 MW;  3F3B3C2724C19208 CRC64;
     MTRSPCSTTS RWISSMSTSE YRAVDAESDL PISAAELAAL ASQLYAASIR PGPDSPPQQA
     PVAPRGSVPD ATAATSAGRT AAGTADVYPG PVPQVGGRDV YLPPPASPAP EAPPQAAPPA
     PRGSAPDATA ATSAGRAAAG TSDVYSSWVP QLGVADIYLG APTPAGPEAP PQSAPPAPRG
     QVPDTTAAAT AYGADLSAFA VPTGIVSTAP GVQAGTAPPV PVVPRAATAP SWLPEAPSVA
     DLGWSDAPAP DAPAGDEHDY HFLTKTDPVP QFRDEHEVFD VAAIRSDFPI LKETVNGKPL
     IWFDNAATTQ KPQVVIDRLS HFYAHENSNI HRAAHELAAR ATDAYEEARD TVAEFIGAPS
     SDNIVFVRGT TEAINLVAHA WGAKHLQPGD EIVITHLEHH ANIVPWQLIS QKTGAILKVA
     PIDDAGNLLL SEFEGLLGPR TKLVAASHVS NALGTVMPVD KIVELGHRYG ARVLIDGAQS
     IQHIPIDVAE LGADFFVFSG HKIYGPTGIG ALYGTEEALT ETPPWQGGGH MIADVTLERS
     LYQGPPTKFE AGTGNIADAV GLTEALRYVQ RLGVERIAAY EHALLEYATP RLADIPGVRL
     IGTAQEKASV LSFVLAGHEP LEVGKALNAE GIAVRAGHHC AQPALRRLGL EATVRPSFAF
     YNTFEEIDVF LRAVRRIAEG GANVG