HYPF_RHOCA
ID HYPF_RHOCA Reviewed; 739 AA.
AC Q02987;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0000250|UniProtKB:P30131};
DE EC=6.2.-.- {ECO:0000250|UniProtKB:P30131};
DE AltName: Full=Carbamoyl phosphate-converting enzyme HypF;
DE AltName: Full=[NiFe]-hydrogenase maturation factor HypF;
DE Short=Hydrogenase maturation protein HypF;
GN Name=hypF;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF C-TERMINUS.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=8497190; DOI=10.1111/j.1365-2958.1993.tb01199.x;
RA Colbeau A., Richaud P., Toussaint B., Caballero F.J., Elster C.,
RA Delphin C., Smith R.L., Chabert J., Vignais P.M.;
RT "Organization of the genes necessary for hydrogenase expression in
RT Rhodobacter capsulatus. Sequence analysis and identification of two hyp
RT regulatory mutants.";
RL Mol. Microbiol. 8:15-29(1993).
RN [2]
RP FUNCTION.
RX PubMed=9492269; DOI=10.1046/j.1432-1327.1998.2510065.x;
RA Colbeau A., Elsen S., Tomiyama M., Zorin N.A., Dimon B., Vignais P.M.;
RT "Rhodobacter capsulatus HypF is involved in regulation of hydrogenase
RT synthesis through the HupUV proteins.";
RL Eur. J. Biochem. 251:65-71(1998).
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases
CC (PubMed:9492269). Along with HypE, it catalyzes the synthesis of the CN
CC ligands of the active site iron of [NiFe]-hydrogenases. HypF functions
CC as a carbamoyl transferase using carbamoylphosphate as a substrate and
CC transferring the carboxamido moiety in an ATP-dependent reaction to the
CC thiolate of the C-terminal cysteine of HypE yielding a protein-S-
CC carboxamide (By similarity). {ECO:0000250|UniProtKB:P30131,
CC ECO:0000269|PubMed:9492269}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + C-terminal L-cysteinyl-[HypE protein] + carbamoyl
CC phosphate + H2O = AMP + C-terminal S-carboxamide-L-cysteinyl-[HypE
CC protein] + diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:55636,
CC Rhea:RHEA-COMP:14247, Rhea:RHEA-COMP:14392, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:76913,
CC ChEBI:CHEBI:139126, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:P30131};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000250|UniProtKB:P30131}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {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; Z15087; CAA78795.1; -; Genomic_DNA.
DR PIR; S32948; S32948.
DR RefSeq; WP_013066510.1; NZ_VIBE01000017.1.
DR AlphaFoldDB; Q02987; -.
DR SMR; Q02987; -.
DR PRIDE; Q02987; -.
DR GeneID; 31489708; -.
DR OMA; VQHHYAH; -.
DR UniPathway; UPA00335; -.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:InterPro.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046944; P:protein carbamoylation; IEA:InterPro.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR InterPro; IPR004421; Carbamoyltransferase_HypF.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR041440; HypF_C.
DR InterPro; IPR006070; YrdC-like_dom.
DR InterPro; IPR011125; Znf_HypF.
DR Pfam; PF00708; Acylphosphatase; 1.
DR Pfam; PF17788; HypF_C; 1.
DR Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR Pfam; PF07503; zf-HYPF; 2.
DR PIRSF; PIRSF006256; CMPcnvr_hdrg_mat; 1.
DR SUPFAM; SSF54975; SSF54975; 1.
DR SUPFAM; SSF55821; SSF55821; 1.
DR TIGRFAMs; TIGR00143; hypF; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 1: Evidence at protein level;
KW Ligase; Metal-binding; Zinc; Zinc-finger.
FT CHAIN 1..739
FT /note="Carbamoyltransferase HypF"
FT /id="PRO_0000071617"
FT DOMAIN 3..87
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT DOMAIN 193..373
FT /note="YrdC-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT ZN_FING 104..128
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P30131"
FT ZN_FING 153..178
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P30131"
FT MUTAGEN 723..739
FT /note="Missing: In RS13 mutant; results in loss of
FT hydrogenase activity."
FT /evidence="ECO:0000269|PubMed:8497190"
SQ SEQUENCE 739 AA; 77879 MW; 19F3AD0C635D90B9 CRC64;
MQAWRIRVRG QVQGVGFRPF VWQLARARGL RGVVLNDAEG VLIRVAGDLG DFAAALRDQA
PPLARVDAVE VTAAVCDDLP EGFQIAASGA AGAETRVTPD AATCPDCLAE IRGEGRRRGY
AFTNCTHCGP RFSILQSLPY DRARTTMAPF AMCPACRAEY EDPADRRFHA QPIACPDCGP
RLWLEAGGAE LPGDAIGLAA ARLKAGEILA VKGLGGFHLA CDATNADAVD LLRARKRRPA
KPFALMAREE DLARIVAVSP AALAALRDPA APIVLMPARG SLPETLAPGM AELGVMLPYT
PLHHLLLDAF GGVLVMTSGN LSGAPQVIGN DEAREKLSAF ADAFLMHDRA IARRLDDSVV
RVDPPMVLRR ARGQVPGTLP LPPGFETAPQ IVAYGGQMKA ALCLIKTGQA LLGHHLGELD
EALTWEAFLQ ADADYAALFD HRPQAVAVDL HPDFRASRHG AARAGRLGVP LIAVQHHHAH
LAACLGENLW PKDGGKVAVI VLDGLGLGPD GTVWGGELLL GDYKGFERVA WLKPAPLIGG
DRAQIEPWRN ALVRLDAAGL SDLADRLFPA APRDLARQLA AKGINAPLSS SAGRLFDAVA
ACLGICPMRQ SYEGEAAMRL ESLAADTGPV PDLPCVGGAI DPAPLFQLLA AGERPDRVAH
ALHASLAQAF AAEARRLIEA GQAEAVALTG GCFQNSRLAT MTRNFLADQG ILTQGRIPAN
DGGLALGQAL VAAAKLESN
