ID   HYPE_AZOVI              Reviewed;         341 AA.
AC   P40595;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 66.
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   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=7906310; DOI=10.1006/jmbi.1994.1149;
RA   Garg R.P., Menon A.L., Jacobs K., Robson R.M., Robson R.L.;
RT   "The hypE gene completes the gene cluster for H2-oxidation in Azotobacter
RT   vinelandii.";
RL   J. Mol. Biol. 236:390-396(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   -!- 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L23970; AAA19513.1; -; Unassigned_DNA.
DR   PIR; S43354; S43354.
DR   RefSeq; WP_012703485.1; NZ_FPKM01000029.1.
DR   AlphaFoldDB; P40595; -.
DR   SMR; P40595; -.
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..341
FT                   /note="Carbamoyl dehydratase HypE"
FT                   /id="PRO_0000201457"
FT   MOD_RES         341
FT                   /note="S-carbamoylcysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P24193"
FT   MOD_RES         341
FT                   /note="S-cyanocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P24193"
SQ   SEQUENCE   341 AA;  36172 MW;  B250404AA9682B75 CRC64;
     MSRLDLRNGS VEMVHGSGGR AMGQLIEELF ARALRNEWLD QRNDQAQFEL PPGRVVMATD
     SHVISPLFFP GGDIGSLAVH GTINDVAMAG ARPCYLAAGF ILEEGFPLAD LARIVESMAA
     AAREAGVPVV TGDTKVVEHG KGDGVFITTT GVGVVPPGLH LSGDQARPGD RILLSGSIGD
     HGVTILSLRE GLGFEADIGS DSQALHGLVA AMLAAVPEIR CLRDPTRGGL GNTLNELARQ
     SGVGMQLVER AIPVREPVRA ACEFLGLDPL YVANEGKLIA ICPAERAERL LEAMRAHPQG
     REAAIIGTVV ADEHRFVQME TPFGGSRMVD WLSGEQLPRI C