ID   HYPF_AZOVI              Reviewed;         776 AA.
AC   P40596;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 3.
DT   25-MAY-2022, entry version 104.
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   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=1610901; DOI=10.1016/0167-4781(92)90077-d;
RA   Chen J.C., Mortenson L.E.;
RT   "Identification of six open reading frames from a region of the Azotobacter
RT   vinelandii genome likely involved in dihydrogen metabolism.";
RL   Biochim. Biophys. Acta 1131:199-202(1992).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA19510.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA45185.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X63650; CAA45185.1; ALT_INIT; Genomic_DNA.
DR   EMBL; L23970; AAA19510.1; ALT_INIT; Unassigned_DNA.
DR   PIR; S23441; S23441.
DR   AlphaFoldDB; P40596; -.
DR   SMR; P40596; -.
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..776
FT                   /note="Carbamoyltransferase HypF"
FT                   /id="PRO_0000071613"
FT   DOMAIN          8..95
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   DOMAIN          204..405
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT   ZN_FING         113..138
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P30131"
FT   ZN_FING         163..188
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250|UniProtKB:P30131"
SQ   SEQUENCE   776 AA;  82733 MW;  E997337C0A15600C CRC64;
     MNQPAEAGVR LLLRGRVQGV GMRPCVHRLA TSLGLAGEVR NTGAGVRIDL LGPPQALAEF
     ERRLPDELPP LARLDAIQRE PLPAGTRFAG FAIAASRDER RGALAPPPDA AVCPACLEEL
     FDPHDRRWRH PFINCTHCGP RYSLIRRLPY DRVQTSLAGF ELCPECRREY EDPADRRFHA
     QPIACPACGP RLCCEDASGR RLSGDPIERA LAALARGEIL ALRGVGGFHL ACDARNAGAV
     AELRRRKRRP AKPFALMAAN PASLQALVEL NENGLAELSG PAAPVVLLRK RPAADDLLAA
     GVAPDLAWLG AMLPHSPLHW LLFHEAAGRP AGTGWAAAPQ DLLLVMTSAN LSGAPPITGN
     AEARERLAGI ADLWLLHDRE ILNRCDDSVV SALGRAPLVI RSGRGLAPLE IPLARGGPSI
     LALGGQLKNA VCLTRGDRAW LSPHNGDLDD ADTCRALERT VARLGELLGI RPERVACDLH
     PDFFASRFAR DYAERHGLPL HPIQHHHAHI AATMAEHGLA EPVLGLALDG FGLGADGRLR
     GGELLRVAAD GCAWLGELNP LPLPGGDQAS REPWRMAAGA LHALGRGGEI ATRFAAEPGN
     AAIARMLERG FNCPPSSSAG RLFDAAAGLL GLGGRQRYEA EAALRLESRV VGLPERVPAL
     WRIDDDNRLD LLPLLARLAD MRDTRAGAEL FHGVLIEALA IWAARAAEAT GLHRVALGGG
     CFLNTVLRDG LCARLRAAGL TPLLARRAPL NDGGLALGQA WAVLLAADIP STRGQA