HYPF_SYNY3
ID HYPF_SYNY3 Reviewed; 767 AA.
AC Q55638;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 135.
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; OrderedLocusNames=sll0322;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA10154.1; -; Genomic_DNA.
DR PIR; S76302; S76302.
DR AlphaFoldDB; Q55638; -.
DR SMR; Q55638; -.
DR IntAct; Q55638; 4.
DR STRING; 1148.1001527; -.
DR PaxDb; Q55638; -.
DR PRIDE; Q55638; -.
DR EnsemblBacteria; BAA10154; BAA10154; BAA10154.
DR KEGG; syn:sll0322; -.
DR eggNOG; COG0068; Bacteria.
DR InParanoid; Q55638; -.
DR OMA; VQHHYAH; -.
DR PhylomeDB; Q55638; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046944; P:protein carbamoylation; IEA:InterPro.
DR GO; GO:0051604; P:protein maturation; IBA:GO_Central.
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; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..767
FT /note="Carbamoyltransferase HypF"
FT /id="PRO_0000071618"
FT DOMAIN 4..90
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT DOMAIN 200..385
FT /note="YrdC-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT ZN_FING 107..132
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P30131"
FT ZN_FING 157..182
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P30131"
SQ SEQUENCE 767 AA; 85358 MW; FA9BA174172AB60D CRC64;
MLKTVAIQVQ GRVQGVGFRP FVYTLAQEMG LNGWVNNSTQ GATVVITADE KAIADFTERL
TKTLPPPGLI EQLAVEQLPL ESFTNFTIRP SSDGPKTASI LPDLSTCSAC LTELFDPSDR
RYLYPFINCT HCGPRYTIIE ALPYDRCRTT MARFRQCTDC EREYKQPGDR RFHAQPNACP
RCGPQLAFWN RQGQVIAEAN EALNFAVDNL KVGNIIAIKG LGGFHLCCDA TDFEAVEKLR
LRKHRPDKPL AVMYGNLGQI VEHYQPNNLE VELLQSAAAP IVLLNKKKQL ILVENIAPGN
PRVGVMLAYT PLHHLLLKKL KKPMVATSGN LAGEQICIDN IDALTRLQNI ADGFLVHDRP
IVCPVDDSVV QIVAGKPLFL RRARGYAPQP ITLPKPTQKK LLAMGGHYKN TVAIAKQNQA
YVSQHLGDLN SAPTYQNFEE AIAHLSQLYD FSPQEIVADL HPDYFSHQYA ENQALPVTFV
QHHYAHILAV MAEHGVMEES VLGIAWDGTG YGMDGTIWGG EFLKITQGTW QRIAHLQPFH
LLGNQQAIKY PHRIALALLW PTFGDDFSAD SLGNWLNFNN GFKNKINSRL NQDLNNKNLR
QLWQRGQAPL TSSMGRLFDG IATLIGLINE VTFEGQAAIA LEAQIMPNLT EEYYPLTLNN
KEKKLAVDWR PLIKAITTED RSKTNLIATK FHNSLVNLII TIAQQQGIEK VALGGGCFQN
CYLLASTITA LKKAGFSPLW PRELPPNDGA ICMGQLLAKI QARQYIC
