HYPE_ECOLI
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 03-AUG-2022, entry version 148.
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}; OrderedLocusNames=b2730, JW2700;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=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: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_LN832404.1.
DR PDB; 2I6R; X-ray; 2.51 A; A/B/C/D=15-336.
DR PDBsum; 2I6R; -.
DR AlphaFoldDB; P24193; -.
DR SMR; P24193; -.
DR BioGRID; 4261424; 23.
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 IntAct; P24193; 10.
DR STRING; 511145.b2730; -.
DR jPOST; P24193; -.
DR PaxDb; P24193; -.
DR PRIDE; P24193; -.
DR EnsemblBacteria; AAC75772; AAC75772; b2730.
DR EnsemblBacteria; BAE76807; BAE76807; BAE76807.
DR GeneID; 947182; -.
DR KEGG; ecj:JW2700; -.
DR KEGG; eco:b2730; -.
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 PhylomeDB; P24193; -.
DR BioCyc; EcoCyc:EG10487-MON; -.
DR BioCyc; MetaCyc:EG10487-MON; -.
DR UniPathway; UPA00335; -.
DR EvolutionaryTrace; P24193; -.
DR PRO; PR:P24193; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1904949; C:ATPase complex; IPI:ComplexPortal.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046892; P:peptidyl-S-carbamoyl-L-cysteine dehydration; IDA:ComplexPortal.
DR GO; GO:0051604; P:protein maturation; IMP:EcoCyc.
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 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 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
