ID   HYPF_AZOCH              Reviewed;         776 AA.
AC   Q43950;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   25-MAY-2022, entry version 99.
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=hupY;
OS   Azotobacter chroococcum mcd 1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8486288; DOI=10.1016/0378-1119(93)90616-b;
RA   Tibelius K.H., Du L., Tito D., Stejskal F.;
RT   "The Azotobacter chroococcum hydrogenase gene cluster: sequences and
RT   genetic analysis of four accessory genes, hupA, hupB, hupY and hupC.";
RL   Gene 127:53-61(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8486288.
RA   Tibelius K.H., Du L., Tito D., Stejskal F.;
RL   Gene 134:141-141(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA22134.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L00674; AAA22134.1; ALT_INIT; Genomic_DNA.
DR   PIR; JN0648; JN0648.
DR   AlphaFoldDB; Q43950; -.
DR   SMR; Q43950; -.
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_0000071612"
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;  82569 MW;  6ACDA50B8F90911B CRC64;
     MNEAAKAGVR LLLRGRVQGV GMRPGVHRLA TSLGLAGAVC NTGEGVRIDL QGPPAALAEF
     ERRLPAELPP LARLDALQRE NLPAGAHFAG FAIVPSRDEA GGALAPPPDA AVCPACLEEL
     FDPHDRRWRH PFINCTHCGP RYSLIRRLPY DRAQTSLAGF ALCPDCRHEY EDPADRRFHA
     QPIACPACGP RLWCEDAAGN RLPGEPVELA LATLRRGEIV ALRGVGGFHL ACDARNAGAV
     ALLRRRKRRP AKPFALMAAN PASLEALVEL NETGLNELSA PAAPVVLLRR RPAADGLLAA
     EVAPDLAWLG VMLPHSPLHW LLFHEAAGRP AGTAWTAAPQ DLVLVMTSAN LSGEPLITGN
     LEAREKLAGI TDLWLLHDRE ILNRVDDSLV NALGRAPVVI RSGRGLAPQE IRLARSGPSV
     LALGGQLKNA ICLTQGDRAW LSPHIGDLHS ADACRSLERT VAQFGELLGV RPERIACDLH
     PDFFASRFAR EHAERHGLPL YPVQHHHAHI AAVLAEHGLA EPVLGLALDG FGLGADGRLR
     GGELLKVAVD GCAWLGELNP LPLPGGDQAA REPWRMAAGA LHALGRGGEI ATRFAAEPGS
     AAIARMLERG FNCPPSSSAG RLFDAAAGLL GLGERQRYEA EAALRLESRI GSLPEAVPPL
     WRIGDDNRLD LSPLLARLAD THDSRVGAEL FHAVLIAALT AWVVRAAAAT GLRRIALGGG
     CFLNTVLRDG LCTRLQAAGL EPLLPRRAPV NDGGLALGQA WVVLLAPDIP STRGQA