ID   HYPE_CUPNH              Reviewed;         351 AA.
AC   P31905; P70739;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 126.
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; OrderedLocusNames=PHG017;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OG   Plasmid megaplasmid pHG1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8352644; DOI=10.1007/bf00249034;
RA   Dernedde J., Eitinger M., Friedrich B.;
RT   "Analysis of a pleiotropic gene region involved in formation of
RT   catalytically active hydrogenases in Alcaligenes eutrophus H16.";
RL   Arch. Microbiol. 159:545-553(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA   Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT   "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT   encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL   J. Mol. Biol. 332:369-383(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 332-351.
RX   PubMed=8021224; DOI=10.1128/jb.176.14.4385-4393.1994;
RA   Lenz O., Schwartz E., Dernedde J., Eitinger M., Friedrich B.;
RT   "The Alcaligenes eutrophus H16 hoxX gene participates in hydrogenase
RT   regulation.";
RL   J. Bacteriol. 176:4385-4393(1994).
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   -!- INTERACTION:
CC       P31905; P45805: hypF1; NbExp=2; IntAct=EBI-2265828, EBI-2265845;
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}.
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DR   EMBL; X70183; CAA49735.1; -; Genomic_DNA.
DR   EMBL; X74670; CAA52734.1; -; Genomic_DNA.
DR   EMBL; AY305378; AAP85773.1; -; Genomic_DNA.
DR   PIR; S29979; S29979.
DR   RefSeq; WP_011153942.1; NZ_CP039289.1.
DR   AlphaFoldDB; P31905; -.
DR   SMR; P31905; -.
DR   IntAct; P31905; 3.
DR   STRING; 381666.PHG017; -.
DR   PRIDE; P31905; -.
DR   EnsemblBacteria; AAP85773; AAP85773; PHG017.
DR   GeneID; 39976672; -.
DR   KEGG; reh:PHG017; -.
DR   PATRIC; fig|381666.6.peg.13; -.
DR   eggNOG; COG0309; Bacteria.
DR   HOGENOM; CLU_049733_0_0_4; -.
DR   OMA; PRVVMGH; -.
DR   OrthoDB; 1016556at2; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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   1: Evidence at protein level;
KW   Lyase; Plasmid; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Carbamoyl dehydratase HypE"
FT                   /id="PRO_0000201455"
FT   MOD_RES         351
FT                   /note="S-carbamoylcysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P24193"
FT   MOD_RES         351
FT                   /note="S-cyanocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P24193"
SQ   SEQUENCE   351 AA;  36596 MW;  35D7291974B7BBBD CRC64;
     MSGTVKLGYQ RPLNIKSGRI DMGHGAGGRA AAQLIQELFV AAFDNEWLRQ GNDQAAFAMP
     AGARMVMATD AHVVSPLFFP GGDIGSLSVH GTINDVAMAG AKPLYLAASF ILEEGFPLAD
     LKRIVESMAG AAREAGVPIV TGDTKVVEQG KGDGVFITTT GVGVVPAGIL IDGAGARPGD
     AILLSGTMGE HGVAILSKRE SLEFDTEIRS DSAALHDLVA QMLAVVPGVR VLRDPTRGGL
     ATTLNEISSQ SGVGMVLDEA AIPVLPQVDA ACELLGLDPL YVANEGKLVA ICAAADADAL
     LAAMRGHPLG REARRIGEVI EDGRHFVQMR TKFGGMRVVD WLSGEQLPRI C