ID   HYPE_ECOLI              Reviewed;         336 AA.
AC   P24193; Q2MA99; Q46886;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   02-SEP-2026, entry version 162.
DE   RecName: Full=Carbamoyl dehydratase HypE {ECO:0000305};
DE            EC=4.2.1.- {ECO:0000269|PubMed:12586941, ECO:0000269|PubMed:15291820};
DE   AltName: Full=Hydrogenase maturation factor HypE {ECO:0000305};
GN   Name=hypE {ECO:0000303|PubMed:1849603};
GN   OrderedLocusNames=b2730, JW2700;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1849603; DOI=10.1111/j.1365-2958.1991.tb01833.x;
RA   Lutz S., Jacobi A., Schlensog V., Boehm R., Sawers G., Boeck A.;
RT   "Molecular characterization of an operon (hyp) necessary for the activity
RT   of the three hydrogenase isoenzymes in Escherichia coli.";
RL   Mol. Microbiol. 5:123-135(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-9, FUNCTION, CATALYTIC ACTIVITY, CARBAMYLATION AT
RP   CYS-336, CYANYLATION AT CYS-336, INTERACTION WITH HYPF, AND MUTAGENESIS OF
RP   ASP-83.
RX   PubMed=15291820; DOI=10.1111/j.1432-1033.2004.04280.x;
RA   Blokesch M., Paschos A., Bauer A., Reissmann S., Drapal N., Boeck A.;
RT   "Analysis of the transcarbamoylation-dehydration reaction catalyzed by the
RT   hydrogenase maturation proteins HypF and HypE.";
RL   Eur. J. Biochem. 271:3428-3436(2004).
RN   [5]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, CARBAMYLATION AT CYS-336, AND CYANYLATION AT
RP   CYS-336.
RX   PubMed=12586941; DOI=10.1126/science.1080972;
RA   Reissmann S., Hochleitner E., Wang H., Paschos A., Lottspeich F.,
RA   Glass R.S., Boeck A.;
RT   "Taming of a poison: biosynthesis of the NiFe-hydrogenase cyanide
RT   ligands.";
RL   Science 299:1067-1070(2003).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH HYPC AND HYPD.
RX   PubMed=15504408; DOI=10.1016/j.jmb.2004.09.040;
RA   Blokesch M., Albracht S.P., Matzanke B.F., Drapal N.M., Jacobi A.,
RA   Boeck A.;
RT   "The complex between hydrogenase-maturation proteins HypC and HypD is an
RT   intermediate in the supply of cyanide to the active site iron of [NiFe]-
RT   hydrogenases.";
RL   J. Mol. Biol. 344:155-167(2004).
RN   [8]
RP   INTERACTION WITH HYBG AND HYPD.
RX   PubMed=16412426; DOI=10.1016/j.febslet.2005.12.063;
RA   Butland G., Zhang J.W., Yang W., Sheung A., Wong P., Greenblatt J.F.,
RA   Emili A., Zamble D.B.;
RT   "Interactions of the Escherichia coli hydrogenase biosynthetic proteins:
RT   HybG complex formation.";
RL   FEBS Lett. 580:677-681(2006).
RN   [9] {ECO:0007744|PDB:2I6R}
RP   X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 15-336, SUBUNIT, AND INTERACTION
RP   WITH HYPF.
RX   PubMed=18065529; DOI=10.1128/jb.01610-07;
RA   Rangarajan E.S., Asinas A., Proteau A., Munger C., Baardsnes J.,
RA   Iannuzzi P., Matte A., Cygler M.;
RT   "Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia
RT   coli and its interaction with HypF.";
RL   J. Bacteriol. 190:1447-1458(2008).
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 (PubMed:12586941, PubMed:15291820). The cyano
CC       group is then transferred from HypE to the HypC-HypD complex or the
CC       HybG-HypD complex (PubMed:15504408). {ECO:0000269|PubMed:12586941,
CC       ECO:0000269|PubMed:15291820, ECO:0000269|PubMed:15504408}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=C-terminal S-carboxamide-L-cysteinyl-[HypE protein] + ATP = C-
CC         terminal S-cyanate-L-cysteinyl-[HypE protein] + ADP + phosphate +
CC         H(+); 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:0000269|PubMed:12586941, ECO:0000269|PubMed:15291820};
CC   -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer (PubMed:18065529). Forms a complex with HypF
CC       (PubMed:15291820, PubMed:18065529). Also forms a complex with HypC, or
CC       HybG, and HypD (PubMed:15504408, PubMed:16412426).
CC       {ECO:0000269|PubMed:15291820, ECO:0000269|PubMed:15504408,
CC       ECO:0000269|PubMed:16412426, ECO:0000269|PubMed:18065529}.
CC   -!- INTERACTION:
CC       P24193; P30131: hypF; NbExp=2; IntAct=EBI-552743, EBI-9128507;
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:0000269|PubMed:12586941,
CC       ECO:0000269|PubMed:15291820}.
CC   -!- SIMILARITY: Belongs to the HypE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69240.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE76807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA38416.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X54543; CAA38416.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U29579; AAA69240.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC75772.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76807.1; ALT_INIT; Genomic_DNA.
DR   PIR; S15201; S15201.
DR   RefSeq; NP_417210.2; NC_000913.3.
DR   RefSeq; WP_001059922.1; NZ_CP009789.1.
DR   PDB; 2I6R; X-ray; 2.51 A; A/B/C/D=15-336.
DR   AlphaFoldDB; P24193; -.
DR   SMR; P24193; -.
DR   BioGRID; 4261424; 24.
DR   BioGRID; 851514; 6.
DR   ComplexPortal; CPX-5281; HypEF Ni-hydrogenase maturation complex.
DR   ComplexPortal; CPX-5283; Hybg-HypDE Ni-hydrogenase maturation complex.
DR   ComplexPortal; CPX-5284; HypCDE Ni-hydrogenase maturation complex.
DR   DIP; DIP-9999N; -.
DR   FunCoup; P24193; 127.
DR   IntAct; P24193; 10.
DR   STRING; 511145.b2730; -.
DR   jPOST; P24193; -.
DR   PaxDb; 511145-b2730; -.
DR   EnsemblBacteria; AAC75772; AAC75772; b2730.
DR   GeneID; 947182; -.
DR   KEGG; ecj:JW2700; -.
DR   KEGG; eco:b2730; -.
DR   KEGG; ecoc:C3026_15020; -.
DR   PATRIC; fig|1411691.4.peg.4011; -.
DR   EchoBASE; EB0482; -.
DR   eggNOG; COG0309; Bacteria.
DR   HOGENOM; CLU_049733_0_0_6; -.
DR   InParanoid; P24193; -.
DR   OMA; CGNGGKE; -.
DR   OrthoDB; 9801934at2; -.
DR   PhylomeDB; P24193; -.
DR   BioCyc; EcoCyc:EG10487-MONOMER; -.
DR   BioCyc; MetaCyc:EG10487-MONOMER; -.
DR   UniPathway; UPA00335; -.
DR   EvolutionaryTrace; P24193; -.
DR   PRO; PR:P24193; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P24193; -.
DR   GO; GO:1904949; C:ATPase complex; IPI:ComplexPortal.
DR   GO; GO:0051604; P:protein maturation; IMP:EcoCyc.
DR   GO; GO:0065003; P:protein-containing complex assembly; IDA:ComplexPortal.
DR   CDD; cd02197; HypE; 1.
DR   FunFam; 3.30.1330.10:FF:000015; Hydrogenase expression/formation protein HypE; 1.
DR   FunFam; 3.90.650.10:FF:000015; Hydrogenase expression/formation protein HypE; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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   NCBIfam; TIGR02124; hypE; 1.
DR   PANTHER; PTHR30303:SF0; CARBAMOYL DEHYDRATASE HYPE; 1.
DR   PANTHER; PTHR30303; HYDROGENASE ISOENZYMES FORMATION PROTEIN HYPE; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   PIRSF; PIRSF005644; Hdrgns_mtr_HypE; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
DR   PDBsum; 2I6R; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Lyase; Reference proteome.
FT   CHAIN           1..336
FT                   /note="Carbamoyl dehydratase HypE"
FT                   /id="PRO_0000201459"
FT   MOD_RES         336
FT                   /note="S-carbamoylcysteine; by HypF; alternate"
FT                   /evidence="ECO:0000269|PubMed:12586941,
FT                   ECO:0000269|PubMed:15291820"
FT   MOD_RES         336
FT                   /note="S-cyanocysteine; by autocatalysis; alternate"
FT                   /evidence="ECO:0000269|PubMed:12586941,
FT                   ECO:0000269|PubMed:15291820"
FT   MUTAGEN         83
FT                   /note="D->N: Lack of ATPase activity."
FT                   /evidence="ECO:0000269|PubMed:15291820"
FT   HELIX           15..27
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          37..42
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           43..49
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          51..60
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           72..85
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          93..101
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           106..122
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          126..135
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          139..153
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          169..174
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           178..188
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           204..207
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   TURN            208..212
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          216..221
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           226..237
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          240..245
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   TURN            246..248
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           253..262
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   TURN            266..268
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          275..279
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           281..283
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           284..292
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           295..297
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          301..309
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          311..315
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   HELIX           317..319
FT                   /evidence="ECO:0007829|PDB:2I6R"
FT   STRAND          321..323
FT                   /evidence="ECO:0007829|PDB:2I6R"
SQ   SEQUENCE   336 AA;  35092 MW;  0811EE415F11AF6C CRC64;
     MNNIQLAHGS GGQAMQQLIN SLFMEAFANP WLAEQEDQAR LDLAQLVAEG DRLAFSTDSY
     VIDPLFFPGG NIGKLAICGT ANDVAVSGAI PRYLSCGFIL EEGLPMETLK AVVTSMAETA
     RAAGIAIVTG DTKVVQRGAV DKLFINTAGM GAIPANIHWG AQTLTAGDVL LVSGTLGDHG
     ATILNLREQL GLDGELVSDC AVLTPLIQTL RDIPGVKALR DATRGGVNAV VHEFAAACGC
     GIELSEAALP VKPAVRGVCE LLGLDALNFA NEGKLVIAVE RNAAEQVLAA LHSHPLGKDA
     ALIGEVVERK GVRLAGLYGV KRTLDLPHAE PLPRIC
//