ID   HYPF_RHILV              Reviewed;         759 AA.
AC   P28156;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 97.
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; Synonyms=hupN;
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].
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).
CC   -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Along with
CC       HypE, it catalyzes the synthesis of the CN ligands of the active site
CC       iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase
CC       using carbamoylphosphate as a substrate and transferring the
CC       carboxamido moiety in an ATP-dependent reaction to the thiolate of the
CC       C-terminal cysteine of HypE yielding a protein-S-carboxamide.
CC       {ECO:0000250|UniProtKB:P30131}.
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}.
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DR   EMBL; X52974; CAA37161.1; -; Genomic_DNA.
DR   PIR; S32875; S32875.
DR   AlphaFoldDB; P28156; -.
DR   SMR; P28156; -.
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   3: Inferred from homology;
KW   Ligase; Metal-binding; Zinc; Zinc-finger.
FT   CHAIN           1..759
FT                   /note="Carbamoyltransferase HypF"
FT                   /id="PRO_0000071616"
FT   DOMAIN          15..99
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   DOMAIN          196..387
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT   ZN_FING         116..141
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P30131"
FT   ZN_FING         166..191
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P30131"
SQ   SEQUENCE   759 AA;  80730 MW;  EACA6D7FEE648730 CRC64;
     MTPSLARQIE SPVRRLRLRV RGAVQGVGFR PFAYRLARAM RLSGFVLNDS AGVLIEIEGR
     DANHFPEAVR TQAPPLARID SIDVLELVPA GGERFEILES LGGRSATRIG ADAATCDGCR
     RELTDPASRF FGYPFVNCTH CGPRFTITRA LPYDRAHTSM ASFPMCRTCA ADYVDPENRR
     FHAEPVACPN CGPRLSHPIK EISARLEGGA IVALKGVGGF HLLCDARNDG AIGLLRLRKA
     GDQKPFAVMV RDIEAARQLA RPNEAEEALL ISPARPIVLV AARAGELSGL IAPGLTRVGL
     MLAYAPVHHL LLDELSRSSP HCHAALVATS ANPGGEPLVA DNDDAGRRLV AIADLVVTHD
     RDIVVRADDS VMQVIDGAPA FIRRARGFVP EPVDLGADGP SVIATGADLK NTICVTRGRE
     AFLSQHIGGL DNAEAIRFQR EVIAHLCSIL DVKPEFAACD LHPDFRSVRT AEGLNLPIVP
     VQHHLAHVAA VVADDRLSGP VLGLALDGHG FGTDGTSWGG EIVVIDHHRW QRAGSLMPLP
     LPSGDRAARE PWRMGVAALQ AAGRIDLAPQ LWPGHSGVTQ LTAMFSGSMP TPVTSSLGRL
     FDAAAAIAGV RLVQDYEGQA AMEFEALVRA PRCLAGGYSI GDGTLDFRPL ILHLAEQGRP
     CGADAADVFH GTLIAGLADW AARGAAARGT RQVALGGGCM MNRVLAAGLA RALRERGLEP
     SLPRLAPAND GGIALGQPAY ARQVIMNEHA SIEENRTCA