ID   HYPE_RHOCA              Reviewed;         340 AA.
AC   P26412;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Carbamoyl dehydratase HypE {ECO:0000250|UniProtKB:P24193};
DE            EC=4.2.1.- {ECO:0000250|UniProtKB:P24193};
DE   AltName: Full=Hydrogenase maturation factor HypE {ECO:0000250|UniProtKB:P24193};
GN   Name=hypE;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=8497190; DOI=10.1111/j.1365-2958.1993.tb01199.x;
RA   Colbeau A., Richaud P., Toussaint B., Caballero F.J., Elster C.,
RA   Delphin C., Smith R.L., Chabert J., Vignais P.M.;
RT   "Organization of the genes necessary for hydrogenase expression in
RT   Rhodobacter capsulatus. Sequence analysis and identification of two hyp
RT   regulatory mutants.";
RL   Mol. Microbiol. 8:15-29(1993).
CC   -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Along with
CC       HypF, it catalyzes the synthesis of the CN ligands of the active site
CC       iron of [NiFe]-hydrogenases. HypE catalyzes the ATP-dependent
CC       dehydration of the carboxamido group attached to its C-terminal
CC       cysteine to a cyano group. {ECO:0000250|UniProtKB:P24193}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + C-terminal S-carboxamide-L-cysteinyl-[HypE protein] =
CC         ADP + C-terminal S-cyanate-L-cysteinyl-[HypE protein] + H(+) +
CC         phosphate; Xref=Rhea:RHEA:55644, Rhea:RHEA-COMP:14247, Rhea:RHEA-
CC         COMP:14248, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:139126, ChEBI:CHEBI:139127, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P24193};
CC   -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC       {ECO:0000250|UniProtKB:P24193}.
CC   -!- PTM: Modified by HypF, which adds a carboxamido group to the thiolate
CC       of the C-terminal cysteine, yielding a protein-S-carboxamide. The
CC       carboxamido group is then dehydrated by HypE itself to yield a protein-
CC       thiocyanate. {ECO:0000250|UniProtKB:P24193}.
CC   -!- SIMILARITY: Belongs to the HypE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA43329.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X61007; CAA43329.1; ALT_INIT; Genomic_DNA.
DR   PIR; S32953; S32953.
DR   RefSeq; WP_013066525.1; NC_014034.1.
DR   AlphaFoldDB; P26412; -.
DR   SMR; P26412; -.
DR   GeneID; 31489723; -.
DR   OMA; CGNGGKE; -.
DR   UniPathway; UPA00335; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd02197; HypE; 1.
DR   Gene3D; 3.30.1330.10; -; 1.
DR   Gene3D; 3.90.650.10; -; 1.
DR   InterPro; IPR011854; HypE.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR016188; PurM-like_N.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   PANTHER; PTHR30303; PTHR30303; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   PIRSF; PIRSF005644; Hdrgns_mtr_HypE; 1.
DR   SUPFAM; SSF55326; SSF55326; 1.
DR   SUPFAM; SSF56042; SSF56042; 1.
DR   TIGRFAMs; TIGR02124; hypE; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..340
FT                   /note="Carbamoyl dehydratase HypE"
FT                   /id="PRO_0000201461"
FT   MOD_RES         340
FT                   /note="S-carbamoylcysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P24193"
FT   MOD_RES         340
FT                   /note="S-cyanocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P24193"
SQ   SEQUENCE   340 AA;  34858 MW;  052F9FC36F235EB8 CRC64;
     MALRDERVTL AHGGGGKAMR DLIEEVFTSV FQPPGMEDQA RLTEAALAEP GARLAFTTDS
     YVVTPVEFPG GDIGKIAVCG TVNDLAVGGA RPLWLSAAFI LEEGTEVALL RRIVATMARE
     AEAAGVRIVT GDTKVVGRGA CDGVFVTTSG VGVIPPGREM AAGRVRPGDV AIVNGVLGDH
     GATILAARGD LALTSDIESD CAALGHLMAD VIAAAPGIRA ARDLTRGGLA SALNEIAQTA
     GCGLVIEETA LPLRPEVVGL CEILGLDPLY LANEGRLVVF VPEAEAAAAL AAMRARPEGA
     GACVVGRAVA EHAGQVRMRT AFGGARIVDM LVGEQLPRIC