HYPE_RHILV
ID HYPE_RHILV Reviewed; 350 AA.
AC P40599;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 69.
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 {ECO:0000303|PubMed:8326860};
OS Rhizobium leguminosarum bv. viciae.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=128c53;
RX PubMed=8326860; DOI=10.1111/j.1365-2958.1993.tb01591.x;
RA Rey L., Murillo J., Hernando Y., Hidalgo E., Cabrera E., Imperial J.,
RA Ruiz-Argueso T.;
RT "Molecular analysis of a microaerobically induced operon required for
RT hydrogenase synthesis in Rhizobium leguminosarum biovar viciae.";
RL Mol. Microbiol. 8:471-481(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B10;
RA Brito B., Palacios J.M., Imperial J., Ruiz-Argueso T., Yang W.C.,
RA Bisseling T., Schmitt H., Kerl V., Bauer T., Kokotek W., Lotz W.;
RT "Organization of the hup-region and its differential transcription in non-
RT symbiotic and symbiotic cells of Rhizobium leguminosarum bv. viciae B10.";
RL Mol. Plant Microbe Interact. 8:235-240(1997).
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 -!- DISRUPTION PHENOTYPE: Insertion mutant lacks any hydrogenase activity
CC in symbiosis with peas, but is still able to synthesize the polypeptide
CC for the hydrogenase large subunit. {ECO:0000269|PubMed:8326860}.
CC -!- SIMILARITY: Belongs to the HypE family. {ECO:0000305}.
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DR EMBL; X52974; CAA37164.1; -; Genomic_DNA.
DR EMBL; Z36982; CAA85445.1; -; Genomic_DNA.
DR PIR; S32878; S32878.
DR RefSeq; WP_018517062.1; NZ_WIEJ01000010.1.
DR AlphaFoldDB; P40599; -.
DR SMR; P40599; -.
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..350
FT /note="Carbamoyl dehydratase HypE"
FT /id="PRO_0000201460"
FT MOD_RES 350
FT /note="S-carbamoylcysteine"
FT /evidence="ECO:0000250|UniProtKB:P24193"
FT MOD_RES 350
FT /note="S-cyanocysteine"
FT /evidence="ECO:0000250|UniProtKB:P24193"
SQ SEQUENCE 350 AA; 36457 MW; 778EB9A087982788 CRC64;
MNMMIKAYKR KLDVANGRID LSHGAGGRAM GQLIEGIFHK AFDNDWLRAG NDQSAFSVPG
GRMVMTTDGY VVSPLFFPGG NIGTLAVHGT INDIAMAGAV PLYLSASFII EEGFPLVDLE
RIADSMGAAS REAGVPIITG DTKVVERGKA DGVFISTAGI GMAPDGLDLR SDAARPGDAV
IISGSIGDHG VAVMSKRENL EFDTDIVSDS AALHGLVADM VAAGGAHIRL MRDPTRGGIA
ATLNEIASQS RVGFRIDEEA IPMKPEVAAA CEFLGLDPLN VANEGKLVAV VAPEGADAVL
AAIHAHPLGA EAALIGHVVA DDNYFVQMVT SFGGGRIVDW LSGEQLPRIC
